Cтруктурные основы функционального разнообразия протеолитических ферментов
Диссертация
Значительный практический интерес представляют охарактеризованные в работе новые протеолитические ферменты и их штаммы-продуценты. Так, глутамилэндопептидаза В. intermedius может быть использована для ограниченного протеолиза полипептидов при определении первичной структуры, доменной организации и идентификации белков, а также для сиквенс-специфического гидролиза слитых белков и получения… Читать ещё >
Содержание
- 1. Введение
- 2. Обзор литературы
- 2. 1. Пропептиды как модуляторы функциональной активности протеаз
- 2. 1. 1. Пропептиды и их основные функции
- 2. 1. 2. Пропептиды, участвующие в сворачивании белков
- 2. 1. 3. Пропептиды, поддерживающие белок в неактивном состоянии
- 2. 1. 4. Пропептиды, участвующие в сортировке белков
- 2. 1. 5. Пропептиды, обеспечивающие взаимодействия предшественника с другими молекулами или надмолекулярными структурами
- 2. 1. 6. Изменчивость пропептидов
- 2. 1. 7. Пропептиды и инженерия белков
- 2. 1. 8. Перспективы исследований пропептидов
- 2. 1. 9. Термолизинподобные протеазы как модель для исследования механизмов функционирования пропоследовательностей
- 2. 2. Глутамилэндопептидазы: связь между созреванием предшественника и субстратной специфичностью зрелой протеазы
- 2. 2. 1. Глутамилэндопептидазы — члены структурного семейства химотрипсина
- 2. 2. 2. Структурные детерминанты субстратной специфичности химотрипсинподобных ферментов
- 2. 2. 3. Общая характеристика глутамилэндопептидаз
- 2. 2. 4. Глутамилэндопептидаза Streptomyces griseus
- 2. 2. 5. Вирусные ЗС-подобные сериновые протеазы
- 2. 2. 6. Моделирование пространственных структур глутамилэндопептидаз
- 2. 2. 7. Эпидермолитичекие токсины стафилококков
- 2. 2. 8. Глутамилэндопептидазы бацилл и стафилококковые Glu-специфичные протеазы, не являющиеся эпидермолитическими токсинами
- 2. 2. 9. Глутамилэндопептидазы — связь между созреванием предшественника и субстратной специфичностью
- 2. 2. 10. Перспективы исследования глутамилэндопептидаз
- 2. 1. Пропептиды как модуляторы функциональной активности протеаз
- 3. 1. Реактивы и материалы
- 3. 2. Клеточные линии, бактериальные штаммы и плазмиды
- 3. 3. Общие методы
- 3. 3. 1. Питательные среды для культивирования микроорганизмов
- 3. 3. 2. Манипуляции с ДНК
- 3. 3. 3. Манипуляции с белками
- 3. 3. 4. Биоинформатический анализ
- 3. 3. 4. 1. Общие методы
- 3. 3. 4. 2. Анализ структурной организации предшественников термолизинподобных протеаз
- 4. 1. Структурные детерминанты строгой субстратной специфичности глутамилэндопептидаз
- 4. 1. 1. Создание модели исследований
- 4. 1. 1. 1. Выделение и характеристика глутамилэндопептидазы из Thermoactinomyces species
- 4. 1. 1. 2. Клонирование, секвенирование и экспрессия гена глутамилэндопептидазы из BACILLUS INTERMEDIUS
- 4. 1. 2. Модификация субстратсвязывающего сайта глутамилэндопептидазы в. intermedius
- 4. 1. 3. Получение глутамилэндопептидазы в. intermedius с удаленными N-концевыми остатками
- 4. 1. 4. Изучение механизма формирования активной глутамилэндопептидазы в. intermedius
- 4. 1. 4. 1. Влияние модификации остатка в положении (-1) глутамилэндопептидазы в. intermedius на продукцию активного фермента клетками В. subtilis
- 4. 1. 4. 2. Созревание глутамилэндопептидазы В. intermedius in vitro
- 4. 1. 5. Глутамилэндопептидазы: пропептиды и структурные детерминанты субстратной специфичности
- 4. 1. 1. Создание модели исследований
- 4. 2. Термолизинподобные протеазы — модель для исследования модулирующей способности пропептидов
- 4. 2. 1. Характеристика белков семейства М
- 4. 2. 1. 1. Новая нейтральная протеаза Thermoactinomyces species 27а
- 4. 2. 1. 2. Протеализин — металлопротеаза Serratia proteamaculans 94, представляющая новую группу термолизинподобных ферментов
- 4. 2. 2. Создание прототипа ферментного препарата для улучшения качества мясного сырья на основе протеализина
- 4. 2. 3. Структурная организация предшественников термолизинподобных протеаз
- 4. 2. 3. 1. Структура и функции N-концевых регионов предшественников
- 4. 2. 3. 2. Структура и функции С-концевых регионов предшественников
- 4. 2. 3. 3. Термолизинподобные протеазы, кодируемые одним геномом
- 4. 2. 3. 4. Основные итоги анализа первичной структуры предшественников термолизинподобных протеаз
- 4. 2. 4. Участие пропептидов в формировании активной металлопротеазы Thermoactinomyces species
- 4. 2. 5. Процессинг предшественника протеализина
- 4. 2. 6. Пространственная структура предшественника протеализина
- 4. 2. 6. 1. Кристаллизация предшественника протеализина
- 4. 2. 6. 2. Общая характеристика структуры
- 4. 2. 6. 3. Структура каталитического домена
- 4. 2. 6. 4. Структура и взаимодействия пропептида
- 4. 2. 6. 5. Основные итоги анализа пространственной структуры предшественника протеализина
- 4. 2. 1. Анализ функциональной роли пропептида протеализина
- 4. 2. 7. 1. Пропептид протеализина необходим для формирования активного фермента
- 4. 2. 7. 2. Локализация протеализина в клетке
- 4. 2. 8. Биологические функции протеализинподобных протеаз
- 4. 2. 9. Термолизинподобные протеазы — модель для исследования функций пропептидов
- 4. 2. 1. Характеристика белков семейства М
Список литературы
- Industrial enzymes: a global strategic business report. San Jose: Global Industry Analysts, Inc., 2011. 447 p.
- Докучаева Г. Рынок ферментов: в ожидании перемен. // 2009. URL: http://www. bioinformatix.ru/interesnoe/ryinok-fermentov-v-ozhidanii-peremen.html (дата обращения 24.02.2012).
- Sternlicht M.D., Werb Z. How matrix metalloproteinases regulate cell behavior. // Annu Rev Cell Dev Biol. 2001. V. 17. P. 463−516.
- Lopez-Otin C., Overall C.M. Protease degradomics: a new challenge for proteomics. // Nat Rev Mol Cell Biol. 2002. V. 3. № 7. P. 509−519.
- Yan S.J., Blomme E.A. In situ zymography: a molecular pathology technique to localize endogenous protease activity in tissue sections. // Vet Pathol. 2003. V. 40. № 3. P. 227−236.
- Von Heijne G. The signal peptide. // J Membr Biol. 1990. V. 115. № 3. P. 195−201.
- Inouye M. Intramolecular chaperone: the role of the pro-peptide in protein folding. // Enzyme. 1991. V. 45. № 5−6. P. 314−321.
- Eder J., Fersht A.R. Pro-sequence-assisted protein folding. // Mol Microbiol. 1995. V. 16. № 4. P. 609−614.
- Shinde U., Inouye M. Intramolecular chaperones: polypeptide extensions that modulate protein folding. // Semin Cell Dev Biol. 2000. V. 11. № 1. P. 35−44.
- Khan A.R., James M.N. Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. // Protein Sci. 1998. V. 7. № 4. P. 815−836.
- Ikemura H., Takagi H., Inouye M. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. // J Biol Chem. 1987. V. 262. № 16. P. 7859−7864.
- Silen J.L., Agard D.A. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. // Nature. 1989. V. 341. № 6241. P. 462−464.
- Silen J.L., Frank D., Fujishige A., Bone R., Agard D.A. Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity. // J Bacteriol. 1989. V. 171. № 3. P. 1320−1325.
- Winther J.R., Sorensen P. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. // Proc Natl Acad Sci U S A. 1991. V. 88. № 20. P. 9330−9334.
- Lee Y.C., Miyata Y., Terada I., Ohta Т., Matsuzawa H. Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli. //Agric Biol Chem. 1991. V. 55. № 12. P. 3027−3032.
- Fabre E., Nicaud J.M., Lopez M.C., Gaillardin C. Role of the proregion in the production and secretion of the Yarrowia lipolytica alkaline extracellular protease. // J Biol Chem. 1991. V. 266. № 6. P. 3782−3790.
- Conner G.E. The role of the cathepsin D propeptide in sorting to the lysosome. // J Biol Chem. 1992. V. 267. № 30. P. 21 738−21 745.
- Rehemtulla A., Dorner A.J., Kaufman R.J. Regulation of PACE propeptide-processing activity: requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation. // Proc Natl Acad Sci USA. 1992. V. 89. № 17. P. 8235−8239.
- Fukuda R., Horiuchi H., Ohta A., Takagi M. The prosequence of Rhizopus niveus aspartic proteinase-I supports correct folding and secretion of its mature part in Saccharomyces cerevisiae. // J Biol Chem. 1994. V. 269. № 13. P. 9556−9561.
- Ohnishi Y., Nishiyama M., Horinouchi S., Beppu T. Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme. // J Biol Chem. 1994. V. 269. № 52. P. 32 800−32 806.
- Chang S.C., Chang PC., Lee Y.H. The roles of propeptide in maturation and secretion of Npr protease from Streptomyces. // J Biol Chem. 1994. V. 269. № 5. P. 3548−3554.
- Tao K., Stearns N.A., Dong J., Wu Q.L., Sahagian G.G. The proregion of cathepsin L is required for proper folding, stability, and ER exit. //Arch Biochem Biophys. 1994. V. 311. № l.P. 19−27.
- Mclver K.S., Kessler E., Olson J.C., Ohman D.E. The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. // Mol Microbiol. 1995. V. 18. № 5. P. 877−889.
- Chang Y.C., Kadokura H., Yoda K., Yamasaki M. Secretion of active subtilisin YaB by a simultaneous expression of separate pre-pro and pre-mature polypeptides in Bacillus subtilis. // Biochem Biophys Res Commun. 1996. V. 219. № 2. P. 463−468.
- Baier K., Nicklisch S., Maldener I., Lockau W. Evidence for propeptide-assisted folding of the calcium-dependent protease of the cyanobacterium Anabaena. // Eur J Biochem. 1996. V. 241. № 3. P. 750−755.
- Wetmore D.R., Hardman K.D. Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3). // Biochemistry. 1996. V. 35. № 21. P. 6549−6558.
- O’Donohue M.J., Beaumont A. The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro. // J Biol Chem. 1996. V. 271. № 43. P. 26 477−26 481.
- Cawley N.X., Olsen V., Zhang C.F., Chen H.C., Tan M., Loh Y.P. Activation and processing of non-anchored yapsin 1 (Yap3p). // J Biol Chem. 1998. V. 273. № 1. P. 584−591.
- Baardsnes J., Sidhu S., MacLeod A., Elliott J., Morden D., Watson J., Borgford T. Streptomyces griseus protease B: secretion correlates with the length of the propeptide. // J Bacteriol. 1998. V. 180. № 12. P. 3241−3244.
- Nirasawa S., Nakajima Y., Zhang Z.Z., Yoshida M., Hayashi K. Intramolecular chaperone and inhibitor activities of a propeptide from a bacterial zinc aminopeptidase. //Biochem J. 1999. V. 341 (Pt 1). P. 25−31.
- Marie-Claire C., Ruffet E., Beaumont A., Roques B.P. The prosequence ofthermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.//J Mol Biol. 1999. V. 285. № 5. P. 1911−1915.
- Yamamoto Y., Watabe S., Kageyama T., Takahashi S.Y. Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme. // Arch Insect Biochem Physiol. 1999. V. 42. № 3. P. 167−178.
- Lesage G., Prat A., Lacombe J., Thomas D.Y., Seidah N.G., Boileau G. The Kex2p proregion is essential for the biosynthesis of an active enzyme and requires a C-terminal basic residue for its function. // Mol Biol Cell. 2000. V. 11. № 6. P. 1947−1957.
- Wiederanders B. The function of propeptide domains of cysteine proteinases. // Adv Exp Med Biol. 2000. V. 477. P. 261−270.
- Zhang Z.Z., Nirasawa S., Nakajima Y., Yoshida M., Hayashi K. Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolytics. // Biochem J. 2000.V. 350 (Pt3). P. 671−676.
- Tang B., Nirasawa S., Kitaoka M., Hayashi K. The role of the N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition. // Biochem Biophys Res Commun. 2002. V. 296. № 1. P. 78−84.
- Feeney В., Clark A.C. Reassembly of active caspase-3 is facilitated by the propeptide. // J Biol Chem. 2005. V. 280. № 48. P. 39 772−39 785.
- Yasuda Y., Tsukuba Т., Okamoto K., Kadowaki Т., Yamamoto K. The role of the cathepsin E propeptide in correct folding, maturation and sorting to the endosome. // J Biochem (Tokyo). 2005. V. 138. № 5. P. 621−630.
- Muntener K., Willimann A., Zwicky R., Svoboda В., Mach L., Baici A. Folding competence of N-terminally truncated forms of human procathepsin B. // J Biol Chem. 2005. V. 280. № 12. P. 11 973−11 980.
- Gasanov E.V., Demidyuk I.V., Shubin A.V., Kozlovskiy V.l., Leonova O.G., Kostrov S.V. Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius. // Protein Eng Des Sei. 2008. V. 21. № 11. P. 653−658.
- Schilling К., Korner A., Sehmisch S., Kreusch A., Kleint R., Benedix Y., Schlabrakowski A., Wiederanders B. Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases. // Biol Chem. 2009. V. 390. № 2. P. 167−174.
- Safina D., Rafieva L., Demidyuk I., Gasanov E., Chestukhina G., Kostrov S. Involvement of propeptides in formation of catalytically active metalloproteinase from Thermoactinomyces sp. // Protein Pept Lett. 2011. V. 18. № 11. P. 1119−1125.
- Baker D., Shiau A.K., Agard D.A. The role of pro regions in protein folding. // Сип-Орт Cell Biol. 1993. V. 5. № 6. P. 966−970.
- Bryan P.N. Prodomains and protein folding catalysis. // Chem Rev. 2002. V. 102. № 12. P. 4805−4816.
- Демидюк И.В., Заболотская M.B., Велишаева H.C., Сафина Д.Р, Костров C.B. Прозависимый фолдинг микробных протеолитических ферментов. // Мол ген микробиол вирусол. 2003. № 4. Р. 11−15.
- Zhu X.L., Ohta Y., Jordan F., Inouye M. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. //Nature. 1989. V. 339. № 6224. P. 483−484.
- Winther J.R., Sorensen P., Kielland-Brandt M.C. Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion. // J Biol Chem. 1994. V. 269. № 35. P. 22 007−22 013.
- Braun P., Tommassen J., Filloux A. Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. // Mol Microbiol. 1996. V. 19. № 2. P. 297−306.
- Yasukawa K., Kusano M., Inouye K. A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli. // Protein Eng Des Sei. 2007. V. 20. № 8. P. 375−383.
- Bryan P., Alexander P., Strausberg S., Schwarz F., Lan W., Gilliland G., Gallagher D.T. Energetics of folding subtilisin BPN'. // Biochemistry. 1992. V. 31. № 21. P. 4937−4945.
- Ваганова Т.И., Медведева Н. П., Степанов B.M. Ренатурация бактериальных металлопротеиназ. //Биохимия. 1993. Т. 58. № 6. Р. 913−920.
- MatsubaraM., Kurimoto Е., Kojima S., MiuraK., Sakai Т. Achievement ofrenaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor. // FEBS Lett. 1994. V. 342. № 2. P. 193−196.
- Hayashi Т., Matsubara M., Nohara D., Kojima S., Miura K., Sakai T. Renaturation of the mature subtilisin BPN' immobilized on agarose beads. //FEBS Lett. 1994. V. 350. № l. P 109−112.
- Mansfeld J., Petermann E., Durrschmidt P., Ulbrich-Hofmann R. The propeptide is not required to produce catalytically active neutral protease from Bacillus stearothermophilus. // Protein Expr Purif. 2005. V. 39. № 2. P. 219−228.
- Sohl J.L., Jaswal S.S., Agard D.A. Unfolded conformations of alpha-lytic protease are more stable than its native state. //Nature. 1998. V. 395. № 6704. P. 817−819.
- Subbian E., Yabuta Y., Shinde U. Positive selection dictates the choice between kinetic and thermodynamic protein folding and stability in subtilases. // Biochemistry. 2004. V. 43. № 45. P. 14 348−14 360.
- Truhlar S.M., Cunningham E.L., Agard D.A. The folding landscape of Streptomyces griseus protease В reveals the energetic costs and benefits associated with evolving kinetic stability. // Protein Sci. 2004. V. 13. № 2. P. 381−390.
- Eder J., Rheinnecker M., Fersht A.R. Folding of subtilisin BPN': role of the pro-sequence. // J Mol Biol. 1993. V. 233. № 2. P. 293−304.
- Gallagher Т., Gilliland G., Wang L., Bryan P. The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'. // Structure. 1995. V. 3. № 9. P. 907−914.
- Anderson D.E., Peters R.J., Wilk В., Agard D.A. alpha-lytic protease precursor: characterization of a structured folding intermediate. // Biochemistry. 1999. V. 38. № 15. P. 4728−4735.
- Baker D., Agard D.A. Kinetics versus thermodynamics in protein folding. // Biochemistry. 1994. V. 33. № 24. P. 7505−7509.
- Cunningham E.L., Jaswal S.S., Sohl J.L., Agard D.A. Kinetic stability as a mechanism for protease longevity. // Proc Natl Acad Sci USA. 1999. V. 96. № 20. P. 11 008−11 014.
- Jaswal S.S., Sohl J.L., Davis J.H., Agard D.A. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. // Nature. 2002. V. 415. № 6869. P. 343−346.
- Kelch B.A., Agard D.A. Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability. // J Mol Biol. 2007. V. 370. № 4. P. 784−795.
- Shinde U.P., Liu J.J., Inouye M. Protein memory through altered folding mediated by intramolecular chaperones. //Nature. 1997. V. 389. № 6650. P. 520−522.
- Shinde U., Fu X., Inouye M. A pathway for conformational diversity in proteins mediated by intramolecular chaperones. // J Biol Chem. 1999. V. 274. № 22. P. 15 615−15 621.
- Nagayama M., Maeda H., Kuroda K., Ueda M. Mutated intramolecular chaperones generate high-activity isomers of mature enzymes. // Biochemistry. 2012. V. 51. № 17. P. 3547−53.
- Zabolotskaya M.V., Demidyuk I.V., Akimkina T.V., Kostrov S.V. A novel neutral protease from Thermoactinomyces species 27a: sequencing of the gene, purification, and characterization of the enzyme. // Protein J. 2004. 483−492.
- Seidah N.G., Mayer G., Zaid A., Rousselet E., Nassoury N., Poirier S., Essalmani R., Prat A. The activation and physiological functions of the proprotein convertases. // Int J Biochem Cell Biol. 2008. V. 40. № 6−7. P. 1111−1125.
- Muller L., Cameron A., Fortenberry Y., Apletalina E.V., Lindberg I. Processing and sorting of the prohormone convertase 2 propeptide. // J Biol Chem. 2000. V. 275. № 50. P. 39 213−39 222.
- Wang D., Bode W., Huber R. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution. // J Mol Biol. 1985. V. 185. № 3. P. 595−624.
- Wroblowski B., Diaz J.F., Schlitter J., Engelborghs Y. Modelling pathways of alpha-chymotrypsin activation and deactivation. // Protein Eng. 1997. V. 10. № 10. P. 1163−1174.
- Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E. Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. // Proc Natl Acad Sci USA. 1994. V. 91. № 16. P. 7588−7592.
- Stroud R.M., Kossiakoff A. A., Chambers J.L. Mechanisms of zymogen activation. // Annu Rev Biophys Bioeng. 1977. V. 6. P. 177−193.
- Schechter I., Berger A. On the size of the active site in proteases. I. Papain. // Biochem Biophys Res Commun. 1967. V. 27. № 2. P. 157−162.
- Ruthenburger M., Mayerle J., Lerch M.M. Cell biology of pancreatic proteases. // Endocrinol Metab Clin North Am. 2006. V. 35. № 2. P. 313−331.
- Yousef G.M., Diamandis E.P. The new human tissue kallikrein gene family: structure, function, and association to disease. // Endocr Rev. 2001. V. 22. № 2. P. 184−204.
- Yoon H., Laxmikanthan G., Lee J., Blaber S.I., Rodriguez A., Kogot J.M., Scarisbrick I.A., Blaber M. Activation profiles and regulatory cascades of the human kallikrein-related peptidases. // J Biol Chem. 2007. V. 282. № 44. P. 31 852−31 864.
- Cloutier S.M., Chagas J.R., Mach J.P., Gygi C.M., Leisinger H.J., Deperthes D. Substrate specificity of human kallikrein 2 (hK2) as determined by phage display technology. // Eur J Biochem. 2002. V. 269. № 11. P. 2747−2754.
- Memari N., Jiang W., Diamandis E.P., Luo L.Y. Enzymatic properties of human kallikrein-related peptidase 12 (KLK12). // Biol Chem. 2007. V. 388. № 4. P. 427−435.
- Borgono C.A., Gavigan J.A., Alves J., Bowles B., Harris J.L., Sotiropoulou G., Diamandis E.P. Defining the extended substrate specificity of kallikrein 1-related peptidases. //Biol Chem. 2007. V. 388. № 11. P. 1215−1225.
- Li H.X., Hwang B.Y., Laxmikanthan G., Blaber S.I., Blaber M., Golubkov P.A., Ren P., Iverson B.L., Georgiou G. Substrate specificity of human kallikreins 1 and 6 determined by phage display. //Protein Sci. 2008. V. 17. № 4. P. 664−672.
- Yoon H., Blaber S.I., Debela M., Goettig P., Scarisbrick I.A., Blaber M. A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15. // Biol Chem. 2009. V. 390. № 4. P. 373−377.
- Borgono C.A., Diamandis E.P. The emerging roles of human tissue kallikreins in cancer. //Nat Rev Cancer. 2004. V. 4. № 11. P. 876−890.
- Delbaere L.T., Sudom A.M., Prasad L., Leduc Y., Goldie H. Structure/function studies of phosphoryl transfer by phosphoenolpyruvate carboxykinase. // Biochim Biophys Acta. 2004. V. 1697. № 1−2. P. 271−278.
- Park C.H., Lee S.J., Lee S.G., Lee W.S., Byun S.M. Hetero- and autoprocessing of the extracellular metalloprotease (Mpr) in Bacillus subtilis. // J Bacteriol. 2004. V. 186. № 19. P. 6457−6464.
- Велишаева H.C., Гасанов E.B., Громова Т. Ю., Демидкж И. В. Влияние модификации сайта процессинга глутамилэндопептидазы Bacillus intermedius на продукцию активного фермента клетками Bacillus subtilis. // Биоорг химия. 2008. Т. 34. № 6. Р. 786−791.
- Baker D., Silen J.L., Agard D.A. Protease pro region required for folding is a potent inhibitor of the mature enzyme. //Proteins. 1992. V. 12. № 4. P. 339−344.
- Ohta Y., Hojo H., Aimoto S., Kobayashi Т., Zhu X., Jordan F., Inouye M. Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide. //Mol Microbiol. 1991. V. 5. № 6. P. 1507−1510.
- Hu Z., Haghjoo K., Jordan F. Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin. // J Biol Chem. 1996. V. 271. № 7. P. 3375−3384.
- Markaryan A., Lee J.D., SirakovaT.D., Kolattukudy P.E. Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides. // J Bacteriol. 1996. V. 178. № 8. P. 2211−2215.
- Taylor M.A., Lee M.J. Trypsin isolated from the midgut of the tobacco hornworm, Manduca sexta, is inhibited by synthetic pro-peptides in vitro. // Biochem Biophys Res Commun. 1997. V. 235. № 3. P. 606−609.
- Boudreault A., Gauthier D., Lazure C. Proprotein convertase PCl/3-related peptides are potent slow tight-binding inhibitors of murine PC 1/3 and Hfurin. // J Biol Chem. 1998. V. 273. № 47. P. 31 574−31 580.
- Lesage G., Tremblay M., Guimond J., Boileau G. Mechanism of Kex2p inhibition by its proregion. // FEBS Lett. 2001. V. 508. № 3. P. 332−336.
- Fugere M., Limperis P.C., Beaulieu-Audy V., Gagnon F., Lavigne P., Klarskov K., Leduc R., Day R. Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains. // J Biol Chem. 2002. V. 277. № 10. P. 7648−7656.
- Golabek A.A., Dolzhanskaya N., Walus M., Wisniewski K.E., Kida E. Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme. // J Biol Chem. 2008. V. 283. № 24. P. 16 497−16 504.
- Fox T., de Miguel E., Mort J.S., Storer A.C. Potent slow-binding inhibition of cathepsin B by its propeptide. // Biochemistry. 1992. V. 31. № 50. P. 12 571−12 576.
- Carmona E., Dufour E., Plouffe C., Takebe S., Mason P., Mort J.S., Menard R. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. // Biochemistry. 1996. V. 35. № 25. P. 8149−8157.
- Maubach G., Schilling K., Rommerskirch W., Wenz I., Schultz J.E., Weber E., Wiederanders B. The inhibition of cathepsin S by its propeptide specificity and mechanism of action. // Eur J Biochem. 1997. V. 250. № 3. P. 745−750.
- Roche L., Tort J., Dalton J.P. The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme. // Mol Biochem Parasitol. 1999. V. 98. № 2. P. 271−277.
- Guay J., Falgueyret J.P., Ducret A., Percival M.D., Mancini J.A. Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. // Eur J Biochem. 2000. V. 267. № 20. P. 6311−6318.
- Billington C.J., Mason P., Magny M.C., Mort J.S. The slow-binding inhibition of cathepsin K by its propeptide. // Biochem Biophys Res Commun. 2000. V. 276. № 3. P. 924−929.
- Sijwali P. S., Shenai B.R., Rosenthal P.J. Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. // J Biol Chem. 2002. V. 277. № 17. P. 14 910−14 915.
- Silva F.B., Batista J.A., Marra B.M., Fragoso R.R., Monteiro A.C., Figueira E.L., Grossi-de-Sa M.F. Pro domain peptide of HGCP-Iv cysteine proteinase inhibits nematode cysteine proteinases. // Genet Mol Res. 2004. V. 3. № 3. P. 342−355.
- Burden R.E., Snoddy P., Jefferies C.A., Walker B., Scott C.J. Inhibition of cathepsin L-like proteases by cathepsin V propeptide. // Biol Chem. 2007. V. 388. № 5. P. 541−545.
- Pandey K.C., Barkan D.T., Sali A., Rosenthal P.J. Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum. // PLoS One. 2009. V. 4. № 5. P. e5694.
- Fusek M., Mares M., Vagner J., Voburka Z., Baudys M. Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen. // FEBS Lett. 1991. V. 287. № 1−2. P. 160−162.
- Kubota K., Nishii W., Kojima M., Takahashi K. Specific inhibition and stabilization of aspergilloglutamic peptidase by the propeptide. Identification of critical sequences and residues in the propeptide. // J Biol Chem. 2005. V. 280. № 2. P. 999−1006.
- Kessler E., Safrin M. The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor. // J Biol Chem. 1994. V. 269. № 36. P. 22 726−22 731.
- Serkina A.V., Gorozhankina T.F., Shevelev A.B., Chestukhina G.G. Propeptide of the metalloprotease of Brevibacillus brevis 7882 is a strong inhibitor of the mature enzyme. // FEBS Lett. 1999. V. 456. № 1. P. 215−219.
- Gonzales P.E., Solomon A., Miller A.B., Leesnitzer M.A., Sagi I., Milla M.E. Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain. // J Biol Chem. 2004. V. 279. № 30. P. 31 638−31 645.
- Demidyuk I.V., Gromova T.Y., Polyakov K.M., Melik-Adamyan W.R., Kuranova I.P., Kostrov S.V. Crystal structure of the protealysin precursor: insights into propeptide function. //J Biol Chem. 2010. V. 285. № 3. P. 2003−2013.
- Li Y., Hu Z., Jordan F., Inouye M. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. // J Biol Chem. 1995. V. 270. № 42. P. 25 127−25 132.
- Wang L., Ruvinov S., Strausberg S., Gallagher D.T., Gilliland G., Bryan P.N. Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding. // Biochemistry. 1995. V. 34. № 47. P. 15 415−15 420.
- Braun P., Bitter W., Tommassen J. Activation of Pseudomonas aeruginosa elastase in Pseudomonas putida by triggering dissociation of the propeptide-enzyme complex. // Microbiology. 2000. V. 146 (Pt 10). P. 2565−2572.
- Bever R.A., Iglewski B.H. Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene. // J Bacteriol. 1988. V. 170. № 9. P. 4309−4314.
- Kessler E., Safrin M. Synthesis, processing, and transport of Pseudomonas aeruginosa elastase. //J Bacteriol. 1988. V. 170. № 11. P. 5241−5247.
- Braun P., de Groot A., Bitter W., Tommassen J. Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. // J Bacteriol. 1998. V. 180. № 13. P. 3467−3469.
- Lin L., Lobel P. Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis. // Biochem J. 2001. V. 357 (Pt 1). P. 49−55.
- Golabek A.A., Kida E., Walus M., Wujek P., Mehta P., Wisniewski K.E. Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I. // J Biol Chem. 2003. V. 278. № 9. P. 7135−7145.
- Golabek A.A., Wujek P., Walus M., Bieler S., Soto C., Wisniewski K.E., Kida E. Maturation of human tripeptidyl-peptidase I in vitro. // J Biol Chem. 2004. V. 279. № 30. P. 31 058−31 067.
- Golabek A.A., Kida E. Tripeptidyl-peptidase I in health and disease. // Biol Chem. 2006. V. 387. № 8. P. 1091−1099.
- Johnson L.M., Bankaitis V.A., Emr S.D. Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease. // Cell. 1987. V. 48. № 5. P. 875−885.
- Pohlner J., Halter R., Beyreuther K., Meyer T.F. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. // Nature. 1987. V. 325. № 6103. P. 458−462.
- Vails L.A., Hunter C.P., Rothman J.H., Stevens T.H. Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. // Cell. 1987. V. 48. № 5. P. 887−897.
- Klionsky D.J., Banta L.M., Emr S.D. Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. //Mol Cell Biol. 1988. V. 8. № 5. P. 2105−2116.
- Vails L.A., Winther J.R., Stevens T.H. Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. // J Cell Biol. 1990. V. 111. № 2. P. 361−368.
- Manser E., Fernandez D., Lim L. Processing and secretion of human carboxypeptidase E by C6 glioma cells. // Biochem J. 1991. V. 280 (Pt 3). P. 695−701.
- Fabre E., Tharaud C., Gaillardin C. Intracellular transit of a yeast protease is rescued by trans-complementation with its prodomain. // J Biol Chem. 1992. V. 267. № 21. P. 15 049−15 055.
- Wetmore D.R., Wong S.L., Roche R.S. The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus. // Mol Microbiol. 1992. V. 6. № 12. P. 1593−1604.
- Mclntyre G.F., GodboldG.D., EricksonA.H. ThepH-dependent membrane association of procathepsin L is mediated by a 9-residue sequence within the propeptide. // J Biol Chem. 1994. V. 269. № 1. P. 567−572.
- Takeshima H., Sakaguchi M., Mihara K., Murakami K., Omura T. Intracellular targeting of lysosomal cathepsin D in COS cells. // J Biochem (Tokyo). 1995. V. 118. № 5. P. 981−988.
- Taylor N.A., Shennan K.I., Cutler D.F., Docherty K. Mutations in the pro-peptide of PC2 prevent transit through the secretory pathway. // Biochem Soc Trans. 1996. V. 24. № 2. P. 193S.
- Kim D.W., Lee Y.C., Matsuzawa H. Role of the COOH-terminal pro-sequence of aqualysin I (a heat-stable serine protease) in its extracellular secretion by Thermus thermophilus. // FEMS Microbiol Lett. 1997. V. 157. № 1. P. 39−45.
- Kim D.W., Matsuzawa H. Requirement for the COOH-terminal pro-sequence in the translocation of aqualysin I across the cytoplasmic membrane in Escherichia coli. // Biochem Biophys Res Commun. 2000. V. 277. № 1. P. 216−220.
- Mclver K.S., Kessler E., Ohman D.E. Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities. // Microbiology. 2004. V. 150 (Pt 12). P. 3969−3977.
- Tapper H., Kallquist L., Johnsson E., Persson A.M., Hansson M., Olsson I. Neutrophil elastase sorting involves plasma membrane trafficking requiring the C-terminal propeptide. // Exp Cell Res. 2006. V. 312. № 18. P. 3471−3484.
- Koo B.H., Longpre J.M., Somerville R.P., Alexander J.P., Leduc R., Apte S.S. Regulation of ADAMTS9 secretion and enzymatic activity by its propeptide. // J Biol Chem. 2007. V. 282. № 22. P. 16 146−16 154.
- Yeung P. S., Zagorski N., Marquis H. The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C. // J Bacteriol. 2005. V. 187. № 8. P. 2601−2608.
- Bitar A.P., Cao M., Marquis H. The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis. // J Bacteriol. 2008. V. 190. № 1. P. 107−111.
- Marcusson E.G., Horazdovsky B.F., Cereghino J.L., Gharakhanian E., Emr S.D. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS 10 gene. // Cell. 1994. V. 77. № 4. P. 579−586.
- Mclntyre G.F., Erickson A.H. The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein. //Proc Natl Acad Sci U S A. 1993. V. 90. № 22. P. 10 588−10 592.
- Huete-Perez J.A., Engel J.C., Brinen L.S., Mottram J.C., McKerrow J.H. Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif. // J Biol Chem. 1999. V. 274. № 23. P. 16 249−16 256.
- Muntener K., Zwicky R., Csucs G., Baici A. The alternative use of exons 2 and 3 in cathepsin B mRNA controls enzyme trafficking and triggers nuclear fragmentation in human cells. //Histochem Cell Biol. 2003. V. 119. № 2. P. 93−101.
- Moin K., Demchik L., Mai J., Duessing J., Peters C., Sloane B.F. Observing proteases in living cells. //Adv Exp Med Biol. 2000. V. 477. P. 391−401.
- Baici A., Muntener K., Willimann A., Zwicky R. Regulation of human cathepsin B by alternative mRNA splicing: homeostasis, fatal errors and cell death. // Biol Chem. 2006. V. 387. № 8. P. 1017−1021.
- Muntener K., Zwicky R., Csucs G., Rohrer J., Baici A. Exon skipping of cathepsin B: mitochondrial targeting of a lysosomal peptidase provokes cell death. // J Biol Chem. 2004. V. 279. № 39. P. 41 012−41 017.
- Zwicky R., Muntener K., Csucs G., Goldring M.B., Baici A. Exploring the role of 5' alternative splicing and of the 3'-untranslated region of cathepsin B mRNA. // Biol Chem. 2003. V. 384. № 7. P. 1007−1018.
- Vignon F., Capony F., Chambon M., Freiss G., Garcia M., Rochefort H. Autocrine growth stimulation of the MCF 7 breast cancer cells by the estrogen-regulated 52 K protein. //Endocrinology. 1986. V. 118. № 4. P. 1537−1545.
- Vetvicka V., Vektvickova J., FusekM. Effect of human procathepsin D on proliferation of human cell lines. // Cancer Lett. 1994. V. 79. № 2. P. 131−135.
- Fusek M., Vetvicka V. Mitogenic function of human procathepsin D: the role of the propeptide. // Biochem J. 1994. V. 303 (Pt 3). P. 775−780.
- Vetvicka V., Vetvickova J., Fusek M. Effect of procathepsin D and its activation peptide on prostate cancer cells. // Cancer Lett. 1998. V. 129. № 1. P. 55−59.
- BazzettL.B., WatkinsC.S., Gercel-Taylor C., Taylor D.D. Modulation of proliferation and chemosensitivity by procathepsin D and its peptides in ovarian cancer. // Gynecol Oncol. 1999. V. 74. № 2. P. 181−187.
- Vetvicka V., Vetvickova J., Fusek M. Role of procathepsin D activation peptide in prostate cancer growth. // Prostate. 2000. V. 44. № 1. P. 1−7.
- Vetvicka V., Vetvickova J., Benes P. Role of enzymatically inactive procathepsin D in lung cancer. //Anticancer Res. 2004. V. 24. № 5A. P. 2739−2743.
- Vashishta A., Ohri S.S., Proctor M., Fusek M., Vetvicka V. Role of activation peptide of procathepsin D in proliferation and invasion of lung cancer cells. // Anticancer Res. 2006. V. 26. № 6B. P. 4163−4170.
- Glondu M., Coopman P., Laurent-Matha V., Garcia M., Rochefort H., Liaudet-Coopman E. A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells. // Oncogene. 2001. V. 20. № 47. P. 6920−6929.
- Berchem G., Glondu M., Gleizes M., Brouillet J.P., Vignon F., Garcia M., Liaudet-Coopman E. Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis. // Oncogene. 2002. V. 21. № 38. P. 5951−5955.
- Vetvicka V., Vetvickova J., Hilgert I., Voburka Z., Fusek M. Analysis of the interaction of procathepsin D activation peptide with breast cancer cells. // Int J Cancer. 1997. V. 73. № 3. P. 403−409.
- Laurent-Matha V., Farnoud M.R., Lucas A., Rougeot C., Garcia M., Rochefort H. Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors. //J Cell Sci. 1998. V. Ill (Pt 17). P. 2539−2549.
- Benes P., Vetvicka V., Fusek M. Cathepsin D many functions of one aspartic protease. // Crit Rev Oncol Hematol. 2008. V. 68. № 1. P. 12−28.
- Vetvicka V., Vetvickova J., Fusek M. Anti-human procathepsin D activation peptide antibodies inhibit breast cancer development. // Breast Cancer Res Treat. 1999. V. 57. № 3. P. 261−269.
- Vetvicka V., Benes P., Fusek M. Procathepsin D in breast cancer: what do we know? Effects of ribozymes and other inhibitors. // Cancer Gene Ther. 2002. V. 9. № 10. P. 854−863.
- Ohri S.S., Vashishta A., Proctor M., Fusek M., Vetvicka V. The propeptide of cathepsin D increases proliferation, invasion and metastasis of breast cancer cells. // Int J Oncol. 2008. V. 32. № 2. P. 491−498.
- Journet A., Chapel A., Kieffer S., Louwagie M., Luche S., Garin J. Towards a human repertoire of monocytic lysosomal proteins. // Electrophoresis. 2000. V. 21. № 16. P. 3411−3419.
- Garin J., Diez R., Kieffer S., Dermine J.F., Duclos S., Gagnon E., Sadoul R., Rondeau
- C., Desjardins M. The phagosome proteome: insight into phagosome functions. // J Cell Biol. 2001. V. 152. № 1. P. 165−180.
- Nagler D.K., Kruger S., Kellner A., Ziomek E., Menard R., Buhtz P., Krams M., Roessner A., Kellner U. Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia. // Prostate. 2004. V. 60. № 2. P. 109−119.
- Krueger S., Kalinski Т., Hundertmark Т., Wex Т., Kuster D., Peitz U., Ebert M., Nagler
- D.K., Kellner U., Malfertheiner P, et al. Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer. // J Pathol. 2005. V. 207. № 1. P. 32−42.
- Demidyuk I.V., Gasanov E.V., Safina D.R., Kostrov S.V. Structural organization of precursors of thermolysin-like proteinases. // Protein J. 2008. V. 27. № 6. P. 343−354.
- Fuentes-Prior P., Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. // Biochem J. 2004. V. 384 (Pt 2). P. 201−232.
- Pop C., Salvesen G.S. Human caspases: activation, specificity, and regulation. // J Biol Chem. 2009. V. 284. № 33. P. 21 777−21 781.
- Pop C., Timmer J., Sperandio S., Salvesen G.S. The apoptosome activates caspase-9 by dimerization. // Mol Cell. 2006. V. 22. № 2. P. 269−275.
- Schweigreiter R. The dual nature of neurotrophins. // Bioessays. 2006. V. 28. № 6. P. 583−594.
- Dicou E. Peptides other than the neurotrophins that can be cleaved from proneurotrophins: a neglected story. //Arch Physiol Biochem. 2007. V. 113. № 4−5. P. 228−233.
- Серкина A.B., Шевелев А. Б., Честухина Г. Г. Структура и функции предшественников бактериальных протеиназ. // Биоорг химия. 2001. Т. 27. № 5. Р. 323−346.
- Nakayama К. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. // Biochem J. 1997. V. 327 (Pt 3). P. 625−635.
- Egnell P., Flock J.I. The autocatalytic processing of the subtilisin Carlsberg pro-region is independent of the primary structure of the cleavage site. // Mol Microbiol. 1992. V. 6. № 9. P. 1115−1119.
- Ramos C., Winther J.R. Exchange of regions of the carboxypeptidase Y propeptide. Sequence specificity and function in folding in vivo. // Eur J Biochem. 1996. V. 242. № 1. P. 29−35.
- Van den Hazel H.B., Kielland-Brandt M.C., Winther J.R. Random substitution of large parts of the propeptide of yeast proteinase A. // J Biol Chem. 1995. V. 270. № 15. P. 8602−8609.
- Takagi H., Koga M., Katsurada S., Yabuta Y., Shinde U., Inouye M., Nakamori S. Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones. // FEBS Lett. 2001. V. 508. № 2. P. 210−214.
- Parr-Vasquez C.L., Yada R.Y. Functional chimera of porcine pepsin prosegment and Plasmodium falciparum plasmepsin II. // Protein Eng Des Sel. 2010. V. 23. № 1. P. 19−26.
- Reed J.C., Doctor K.S., Godzik A. The domains of apoptosis: a genomics perspective. // Sci STKE. 2004. V. 2004. № 239. P. re9.
- Delaria K., Fiorentino L., Wallace L., Tamburini P., Brownell E., Muller D. Inhibition of cathepsin L-like cysteine proteases by cytotoxic T-lymphocyte antigen-2 beta. // J Biol Chem. 1994. V. 269. № 40. P. 25 172−25 177.
- Kurata M., Hirata M., Watabe S., Miyake M., Takahashi S.Y., Yamamoto Y. Expression, purification, and inhibitory activities of mouse cytotoxic T-lymphocyte antigen-2alpha. // Protein Expr Purif. 2003. V. 32. № 1. P. 119−125.
- Yamamoto Y., Watabe S., KageyamaT., Takahashi S. Y. Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori. //Arch Insect Biochem Physiol. 1999. V. 42. № 2. P. 119−129.
- Yamamoto Y., Watabe S., Kageyama T., Takahashi S.Y. A novel inhibitor protein for Bombyx cysteine proteinase is homologous to propeptide regions of cysteine proteinases. // FEBS Lett. 1999. V. 448. № 2−3. P. 257−260.
- Yamamoto Y., Kurata M., Watabe S., Murakami R., Takahashi S.Y. Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases. // Curr Protein Pept Sci. 2002. V. 3. № 2. P. 231−238.
- Deshapriya R.M., Takeuchi A., Shirao K., Isa K., Watabe S., Murakami R., Tsujimura H., Yamamoto Y. Drosophila CTLA-2-like protein (D/CTLA-2) inhibits cysteine proteinase 1 (CP1), a cathepsin L-like enzyme. // Zoolog Sci. 2007. V. 24. № 1. P. 21−30.
- Comas D., Petit F., Preat T. Drosophila long-term memory formation involves regulation of cathepsin activity. //Nature. 2004. V. 430. № 6998. P. 460−463.
- Luziga C., Nakamura O., Deshapriya R.M., Usui M., Miyaji M., Wakimoto M., Wada N., Yamamoto Y. Expression mapping of cytotoxic T-lymphocyte antigen-2alpha gene transcripts in mouse brain. // Histochem Cell Biol. 2007. V. 127. № 6. P. 569−579.
- Luziga C., Nakamura O., Deshapriya R.M., Usui M., Miyaji M., Wakimoto M., Wada N., Mbassa G., Yamamoto Y. Dendritic and axonal localization of cytotoxic T-lymphocyte antigen-2 alpha protein in mouse brain. // Brain Res. 2008. V. 1204. P. 40−52.
- Cheon Y.P., DeMayo F.J., Bagchi M.K., Bagchi I.C. Induction of cytotoxic T-lymphocyte antigen-2beta, a cysteine protease inhibitor in decidua: a potential regulator of embryo implantation. // J Biol Chem. 2004. V. 279. № 11. P. 10 357−10 363.
- Campo M.A., Rice E.J., Kasik J.W. There is an increase in expression of the cytotoxic T-lymphocyte antigen-2 alpha gene during pregnancy. // Am J Obstet Gynecol. 1996. V. 174. № 5. P. 1605−1607.
- Jerala R., Zerovnik E., Kidric J., Turk V. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. // J Biol Chem. 1998. V. 273. № 19. P. 11 498−11 504.
- DohmaeN., TakioK., TsumurayaY., Hashimoto Y. The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus. //Arch Biochem Biophys. 1995. V. 316. № 1. P. 498−506.
- Maier K., Muller H., Tesch R., Trolp R., Witt I., Holzer H. Primary structure of yeast proteinase B inhibitor 2. // J Biol Chem. 1979. V. 254. № 24. P. 12 555−12 561.
- Kojima S., Iwahara A., Yanai H. Inhibitor-assisted refolding of protease: a protease inhibitor as an intramolecular chaperone. // FEBS Lett. 2005. V. 579. № 20. P. 4430−4436.
- Fu X., Inouye M., Shinde U. Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked. // J Biol Chem. 2000. V. 275. № 22. P. 16 871−16 878.
- Takagi H., Takahashi M. A new approach for alteration of protease functions: pro-sequence engineering. //Appl Microbiol Biotechnol. 2003. V. 63. № 1. P. 1−9.
- Sidhu S.S., Borgford T.J. Selection of Streptomyces griseus protease B mutants with desired alterations in primary specificity using a library screening strategy. // J Mol Biol. 1996. V. 257. № 2. P. 233−245.
- Visal S., Taylor M.A., Michaud D. The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases. // FEBS Lett. 1998. V. 434. № 3. P. 401−405.
- Plainkum P., Fuchs S.M., Wiyakrutta S., Raines R.T. Creation of a zymogen. // Nat Struct Biol. 2003. V. 10. № 2. P. 115−119.
- Johnson R.J., Lin S.R., Raines R.T. A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus. // FEBS J. 2006. V. 273. № 23. P. 5457−5465.
- Han S., Craig J.A., Putnam C.D., Carozzi N.B., Tainer J.A. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. // Nat Struct Biol. 1999. V. 6. № 10. P. 932−936.
- Jucovic M., Walters F.S., Warren G.W., Palekar N.V., Chen J.S. From enzyme to zymogen: engineering Vip2, an ADP-ribosyltransferase from Bacillus cereus, for conditional toxicity. // Protein Eng Des Sel. 2008. V. 21. № 10. P. 631−638.
- Lazure C. The peptidase zymogen proregions: nature’s way of preventing undesired activation and proteolysis. // Curr Pharm Des. 2002. V. 8. № 7. P. 511−531.
- Wiederanders В., Kaulmann G., Schilling K. Functions of propeptide parts in cysteine proteases. // Curr Protein Pept Sci. 2003. V. 4. № 5. P. 309−326.
- Adekoya O.A., Sylte I. The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential. // Chem Biol Drug Des. 2009. V. 73. № 1. P. 7−16.
- Matthews B.W., Sigler P.B., Henderson R., Blow D.M. Three-dimensional structure of tosyl-alpha-chymotrypsin. //Nature. 1967. V. 214. № 5089. P. 652−656.
- Whitcomb D.C., Lowe M.E. Human pancreatic digestive enzymes. // Dig Dis Sci. 2007. V. 52. № 1. P. 1−17.
- Davie E.W., Fujikawa K., Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. // Biochemistry. 1991. V. 30. № 43. P. 10 363−10 370.
- Barry M., Bleackley R.C. Cytotoxic T lymphocytes: all roads lead to death. // Nat Rev Immunol. 2002. V. 2. № 6. P. 401−409.
- Duncan R.C., Wijeyewickrema L.C., Pike R.N. The initiating proteases of the complement system: controlling the cleavage. // Biochimie. 2008. V. 90. № 2. P. 387−395.
- Honda A., Siruntawineti J., Baba T. Role of acrosomal matrix proteases in sperm-zona pellucida interactions. // Hum Reprod Update. 2002. V. 8. № 5. P. 405−412.
- GorbalenyaA., Snijder E. Viral cysteine proteinases. //Perspectives in Drug Discovery and Design. 1996. V. 6. № 1. P. 64−86.
- Bazan J.F., Fletterick R.J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. // Proc Natl Acad Sci USA. 1988. V. 85. № 21. P. 7872−7876.
- Rawlings N.D., Barrett A.J. Evolutionary families of peptidases. // Biochem J. 1993. V. 290 (Pt 1). P. 205−218.
- Rawlings N.D., Barrett A. J., Bateman A. MEROPS: the peptidase database. //Nucleic Acids Res. 2010. V. 38. № Database issue. P. D227−233.
- Stroud R.M. A family of protein-cutting proteins. // Sci Am. 1974. V. 231. № 1. P. 74−88.
- Руденская Т.Н. Брахиурины сериновые коллагенолитические ферменты крабов. // Биоорг химия. 2003. Т. 29. № 2. Р. 117−128.
- Polanowska J., Krokoszynska I., Czapinska H., Watorek W., Dadlez M., Otlewski J. Specificity of human cathepsin G. // Biochim Biophys Acta. 1998. V. 1386. № 1. P. 189−198.
- Ziebuhr J., Snijder E.J., Gorbalenya A.E. Virus-encoded proteinases and proteolytic processing in the Nidovirales. // J Gen Virol. 2000. V. 81. (Pt 4). P. 853−879.
- Czapinska H., Otlewski J. Structural and energetic determinants of the SI-site specificity in serine proteases. // Eur J Biochem. 1999. V. 260. № 3. P. 571−595.
- Hedstrom L. Trypsin: a case study in the structural determinants of enzyme specificity. // Biol Chem. 1996. V. 377. № 7−8. P. 465−470.
- Hedstrom L. Serine protease mechanism and specificity. // Chem Rev. 2002. V. 102. № 12. P. 4501−4524.
- Perona J.J., Craik C.S. Structural basis of substrate specificity in the serine proteases. // Protein Sci. 1995. V. 4. № 3. P. 337−360.
- Perona J.J., Craik C.S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. // J Biol Chem. 1997. V. 272. № 48. P. 29 987−29 990.
- Knowles J.R. Enzyme specificity: alpha-chymotrypsin. // J Theor Biol. 1965. V. 9. № 2. P. 213−228.
- Dorovska V.N., Varfolomeyev S.D., Kazanskaya N.F., Klyosov A.A., Martinek K. The influence of the geometric properties of the active centre on the specificity of chymotrypsin catalysis. //FEBS Lett. 1972. V. 23. № 1. P. 122−124.
- Blow D. The structure of chymotrypsin, in The Enzymes., P. Boyer, Editor. 1971, New York. p. 185.
- Krieger M., Kay L.M., Stroud R.M. Structure and specific binding of trypsin: comparison of inhibited derivatives and a model for substrate binding. // J Mol Biol. 1974. V. 83. № 2. P. 209−230.
- Shotton D.M., Watson H.C. Three-dimensional structure of tosyl-elastase. // Nature. 1970. V. 225. № 5235. P. 811−816.
- Waugh S.M., Harris J.L., Fletterick R., Craik C.S. The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity. // Nat Struct Biol. 2000. V. 7. № 9. P. 762−765.
- Tsu C.A., Perona J. J., Fletterick R. J., Craik C.S. Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease 1. // Biochemistry. 1997. V. 36. № 18. P. 5393−5401.
- Pletnev V.Z., Zamolodchikova T.S., Pangborn W.A., Duax W.L. Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities. // Proteins. 2000. V. 41. № 1. P. 8−16.
- Hedstrom L., Szilagyi L., Rutter W.J. Converting trypsin to chymotrypsin: the role of surface loops. // Science. 1992. V. 255. № 5049. P. 1249−1253.
- Graf L., Jancso A., Szilagyi L., Hegyi G., Pinter K., Naray-Szabo G., Hepp J., Medzihradszky K., Rutter W.J. Electrostatic complementarity within the substrate-binding pocket of trypsin. // Proc Natl Acad Sci USA. 1988. V. 85. № 14. P. 4961−4965.
- Hedstrom L., Perona J.J., Rutter W.J. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. // Biochemistry. 1994. V. 33. № 29. P. 8757−8763.
- Hedstrom L., Farr-Jones S., Kettner C.A., Rutter W.J. Converting trypsin to chymotrypsin: ground-state binding does not determine substrate specificity. // Biochemistry. 1994. V. 33. № 29. P. 8764−8769.
- Perona J.J., Hedstrom L., Rutter W.J., Fletterick R.J. Structural origins of substrate discrimination in trypsin and chymotrypsin. // Biochemistry. 1995. V. 34. № 5. P. 1489−1499.
- Drapeau G.R., Boily Y., Houmard J. Purification and properties of an extracellular protease of Staphylococcus aureus. // J Biol Chem. 1972. V. 247. № 20. P. 6720−6726.
- Dancer S.J., Garratt R., Saldanha J., Jhoti H., Evans R. The epidermolytic toxins are serine proteases. // FEBS Lett. 1990. V. 268. № 1. P. 129−132.
- HanakawaY., SchechterN.M., LinC., NishifujiK., AmagaiM., StanleyJ.R.Enzymatic and molecular characteristics of the efficiency and specificity of exfoliative toxin cleavage of desmoglein 1. // J Biol Chem. 2004. V. 279. № 7. P. 5268−5277.
- Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S., Kimura S. Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. // Microb Pathog. 2002. V. 33. № 1. P. 33−41.
- Yokoi К., KakikawaM., KimotoH., WatanabeК., YasukawaH., YamakawaA., Taketo A., KodairaK.I. Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M. // Gene. 2001. V. 281. № 1−2. P. 115−122.
- Ono Т., Ohara-Nemoto Y., Shimoyama Y., Okawara H., Kobayakawa Т., Baba T.T., Kimura S., Nemoto Т.К. Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases. // Biol Chem. 2010. V. 391. № 10. P. 1221−1232.
- Fudaba Y., Nishifuji K., Andresen L.O., Yamaguchi Т., Komatsuzawa H., Amagai M., Sugai M. Staphylococcus hyicus exfoliative toxins selectively digest porcine desmoglein 1. // Microb Pathog. 2005. V. 39. № 5−6. P. 171−176.
- Хайдарова H.B., Руденская Г. Н., Ревина Л. П., Степанов В. М., Егоров Н.С. Glu, Asp-специфичная протеиназа из Streptomycetes thermovulgaris. // Биохимия. 1989. Т. 54. № 1. Р. 46−53.
- Svendsen I., Breddam К. Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. // Eur J Biochem. 1992. V. 204. № 1. P. 165−171.
- Rufo G.A., Jr., Sullivan B.J., Sloma A., Pero J. Isolation and characterization of a novel extracellular metalloprotease from Bacillus subtilis. // J Bacteriol. 1990. V. 172. № 2. P. 1019−1023.
- Leshchinskaya I.B., Shakirov E.V., Itskovitch E.L., Balaban N.P., Mardanova A.M., Sharipova M.R., Viryasov M.B., Rudenskaya G.N., Stepanov V.M. Glutamyl endopeptidase of Bacillus intermedius, strain 3−19. // FEBS Lett. 1997. V. 404. № 2−3. P. 241−244.
- Мосолова O.B., Руденская Т. Н., Степанов В. М., Ходова О. М., Цаплина И.А. Glu, Asp-специфичная протеиназа актиномицетов. // Биохимия. 1987. Т. 52. № 3. Р. 414−422.
- Демидюк И.В., Носовская Е. А., Цаплина И. А., Каравайко Г. И., Костров С. В. Выделение и характеристика сериновой протеиназы из Thermoactinomyces species, относящейся к группе Glu, Asp-специфичных ферментов. // Биохимия. 1997. Т. 62. № 2. Р. 202−207.
- McGavin M.J., Zahradka C., Rice K., Scott J.E. Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease. // Infect Immun. 1997. V. 65. № 7. P. 2621−2628.
- Rice K., Peralta R., Bast D., de Azavedo J., McGavin M.J. Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. // Infect Immun. 2001. V. 69. № 1. P. 159−169.
- Shaw L., Golonka E., Potempa J., Foster S.J. The role and regulation of the extracellular proteases of Staphylococcus aureus. //Microbiology. 2004. V. 150 (Pt 1). P. 217−228.
- Nishifuji K., Sugai M., Amagai M. Staphylococcal exfoliative toxins: «molecular scissors» of bacteria that attack the cutaneous defense barrier in mammals. // J Dermatol Sci. 2008. V. 49. № 1. P. 21−31.
- Шарипова M.P., Балабан Н. П., Габдрахманова JI.А., Шилова М. А., Кадырова Ю. М., Руденская Г. Н., Лещинская И. Б. Гидролитические ферменты и спорообразование у Bacillus intermedius. II Микробиология. 2002. Т. 71. № 4. Р. 494−499.
- Wensvoort G. Lelystad virus and the porcine epidemic abortion and respiratory syndrome. // Vet Res. 1993. V. 24. № 2. P. 117−124.
- MacLachlan N.J., Balasuriya U.B. Equine viral arteritis. //Adv Exp Med Biol. 2006. V. 581. P. 429−433.
- Nienaber V.L., Breddam K., Birktoft J.J. A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding. // Biochemistry. 1993. V. 32. № 43. P. 11 469−11 475.
- Cortes A., Emery D.C., Halsall D.J., Jackson R.M., Clarke A.R., Holbrook J.J. Charge balance in the alpha-hydroxyacid dehydrogenase vacuole: an acid test. // Protein Sci. 1992. V. 1. № 7. P. 892−901.
- Svendsen I., Jensen M.R., Breddam K. The primary structure of the glutamic acid-specific protease of Streptomyces griseus. // FEBS Lett. 1991. V. 292. № 1−2. P. 165−167.
- Sidhu S.S., Kalmar G.B., Borgford T.J. Characterization of the gene encoding the glutamic-acid-specific protease of Streptomyces griseus. //Biochem Cell Biol. 1993. V. 71. № 9−10. P. 454−461.
- Stennicke H.R., Birktoft J. J., Breddam K. Characterization of the SI binding site of the glutamic acid-specific protease from Streptomyces griseus. // Protein Sci. 1996. V. 5. № 11. P. 2266−2275.
- Dougherty W.G., Semler B.L. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. // Microbiol Rev. 1993. V. 57. № 4. P. 781−822.
- Spall V.E., Shanks M., Lomonossoff G.P. Polyprotein Processing as a Strategy for Gene Expression in RNA Viruses. // Seminars in Virology. 1997. V. 8. № 1. P. 15−23.
- Snijder E.J., Wassenaar A.L., van Dinten L.C., Spaan W.J., Gorbalenya A.E. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsinlike enzymes, the 3C-like serine proteases. // J Biol Chem. 1996. V. 271. № 9. P. 4864−4871.
- Mosimann S.C., Cherney M.M., Sia S., Plotch S., James M.N. Refined X-ray crystallographic structure of the poliovirus 3C gene product. // J Mol Biol. 1997. V. 273. № 5. P. 1032−1047.
- Bergmann E.M., Mosimann S.C., Chernaia M.M., Malcolm B.A., James M.N. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. // J Virol. 1997. V. 71. № 3. P. 2436−2448.
- Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., Hilgenfeld R. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. // EMBO J. 2002. V. 21. № 13. P. 3213−3224.
- Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. // Science. 2003. V. 300. № 5626. P. 1763−1767.
- Ziebuhr J., Heusipp G., Siddell S.G. Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase. // J Virol. 1997. V. 71. № 5. P. 3992−3997.
- Nagata K., Yoshida N., Ogata F., Araki M., Noda K. Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8. // J Biochem. 1991. V. 110. № 6. P. 859−862.
- Breddam K., Meldal M. Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. // Eur J Biochem. 1992. V. 206. № 1. P. 103−107.
- Barbosa J.A., Garratt R.C., Saldanha J.W. A structural model for the glutamate-specific endopeptidase from Streptomyces griseus that explains substrate specificity. // FEBS Lett. 1993. V. 324. № 1. P. 45−50.
- Melish M.E., Glasgow L.A. The staphylococcal scalded-skin syndrome. // N Engl J Med. 1970. V. 282. № 20. P. 1114−1119.
- Kapral F.A., Miller M.M. Product of Staphylococcus aureus responsible for the scalded-skin syndrome. // Infect Immun. 1971. V. 4. № 5. P. 541−545.
- Kondo I., Sakurai S., Sarai Y. New type of exfoliatin obtained from staphylococcal strains, belonging to phage groups other than group II, isolated from patients with impetigo and Ritter’s disease. // Infect Immun. 1974. V. 10. № 4. P. 851−861.
- Bailey C.J., Smith T.P. The reactive serine residue of epidermolytic toxin A. // Biochem J. 1990. V. 269. № 2. P. 535−537.
- Prevost G., Rifai S., Chaix M.L., Piemont Y. Functional evidence that the Ser-195 residue of staphylococcal exfoliative toxin A is essential for biological activity. // Infect Immun. 1991. V. 59. № 9. P. 3337−3339.
- Redpath M.B., Foster T.J., Bailey C .J. The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus. // FEMS Microbiol Lett. 1991. V. 65. № 2. P. 151−155.
- Rogolsky M., Wiley B.B., Keyhani M., Glasgow L.A. Interaction of staphylococcal exfoliative toxin with concanavalin A. // Infect Immun. 1974. V. 10. № 6. P. 1260−1265.
- Bailey C.J., de Azavedo J., Arbuthnott J.P. A comparative study of two serotypes of epidermolytic toxin from Staphylococcus aureus. // Biochim Biophys Acta. 1980. V. 624. № l.P. 111−120.
- Arbuthnott J.P., Billcliffe B., Thompson W.D. Isoelectric focusing studies of staphylococcal epidermolytic toxin. // FEBS Lett. 1974. V. 46. № 1. P. 92−95.
- Bailey C.J., Redpath M.B. The esterolytic activity of epidermolytic toxins. //Biochem J. 1992. V. 284 (Pt 1). P. 177−180.
- Vath G.M., Earhart C.A., Rago J.V., Kim M.H., Bohach G.A., Schlievert P.M., Ohlendorf D.H. The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease. // Biochemistry. 1997. V. 36. № 7. P. 1559−1566.
- Vath G.M., Earhart C.A., Monie D.D., Iandolo J. J., Schlievert P.M., Ohlendorf D.H. The crystal structure of exfoliative toxin B: a superantigen with enzymatic activity. // Biochemistry. 1999. V. 38. № 32. P. 10 239−10 246.
- Amagai M., Matsuyoshi N., Wang Z.H., Andl C., Stanley J.R. Toxin in bullous impetigo and staphylococcal scalded-skin syndrome targets desmoglein 1. // Nat Med. 2000. V. 6. № 11. P. 1275−1277.
- Amagai M., Yamaguchi T., Hanakawa Y., Nishifuji K., Sugai M., Stanley J.R. Staphylococcal exfoliative toxin B specifically cleaves desmoglein 1. // J Invest Dermatol. 2002. V. 118. № 5. P. 845−850.
- Ahrens P., Andresen L.O. Cloning and sequence analysis of genes encoding Staphylococcus hyicus exfoliative toxin types А, В, C, and D. // J Bacteriol. 2004. V. 186. № 6. P. 1833−1837.
- Rago J.V., Vath G.M., Bohach G.A., Ohlendorf D.H., Schlievert P.M. Mutational analysis of the superantigen staphylococcal exfoliative toxin A (ETA). // J Immunol. 2000. V. 164. № 4. P. 2207−2213.
- Prasad L., Leduc Y., Hayakawa K., Delbaere L.T. The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus. // Acta Crystallogr D Biol Crystallogr. 2004. V. 60 (Pt 2). P. 256−259.
- Drapeau G.R. Role of metalloprotease in activation of the precursor of staphylococcal protease. // J Bacteriol. 1978. V. 136. № 2. P. 607−613.
- Trachuk L.A., Shcheglov A.S., Milgotina E.I., Chestukhina G.G. In vitro maturation pathway of a glutamyl endopeptidase precursor from Bacillus licheniformis. // Biochimie. 2005. V. 87. № 6. P. 529−537.
- Nemoto Т.К., Ohara-Nemoto Y., Ono Т., Kobayakawa Т., Shimoyama Y., Kimura S., Takagi T. Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. // FEBS J. 2008. V. 275. № 3. P. 573−587.
- Балабан Н.П., Марданова A.M., Шарипова M.P., Габдрахманова JI.A., Соколова Е. А., Руденская Г. Н., Лещинская И. Б. Получение и характеристика тиолзависимой сериновой протеиназы 2 Bacillus intermedius 3−19. // Биохимия. 2004. Т. 69. № 4. Р. 519−526.
- Yang M.Y., Ferrari Е., Henner D.J. Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation. //J Bacteriol. 1984. V. 160. № 1. P. 15−21.
- Сорокин А.В., Хазак В. Э. Экспрессионная единица в области инициации репликации плазмиды pSM19035 стрептококов. // Мол биол. 1990. Т. 24. № 4. Р. 993−1000.
- Sambrook J., Fritsch E.F., Maniatis Т. Molecular Cloning: A Laboratory Manual. New York: Cold Spring Harbor Laboratory, 1982. 545 p.
- Anagnostopoulos С., Spizizen J. Requirements for Transformation in Bacillus Subtilis. // J Bacteriol. 1961. V. 81. № 5. P. 741−746.
- Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. //Nature. 1970. V. 227. № 5259. P. 680−685.
- Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. //Anal Biochem. 1987. V. 166. № 2. P. 368−379.
- Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. // Anal Biochem. 1976. V. 72. P. 248−254.
- Гаспаров B.C., Дягтярь В. Г. Определение белка по связыванию с красителем кумасси бриллиантовым голубым G-250. // Биохимия. 1994. Т. 59. № 6. Р. 763−777.
- Dawson М.С., Elliott D.C., Elliott W.H., Jones K.M. Data for Biochemical Research. 3rd ed. Oxford: Clarendon Press, 1989. 592 p.
- Charney J., Tomarelli R.M. Determination of the proteolytic activity of duodenal juice. // J. Biochem. 1947. V. 177. P. 501−505.
- Ревина Л.П., Хайдарова H.B., Руденская Г. Н., Гребенщиков Н. И., Баратова Л. А., Степанов В. М. Исследование действия Glu, Asp-специфичной протеиназы Streptomyces thermovulgaris на пептидные и белковые субстраты. // Биохимия. 1989. Т. 54. № 5. Р. 846−850.
- Bendtsen J.D., Nielsen H., von Heijne G., Brunak S. Improved prediction of signal peptides: SignalP 3.0. // J. Mol. Biol. 2004. V. 340. № 4. P. 783−795.
- Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. // Nucleic Acids Res. 1997. V. 25. № 24. P. 4876−4882.
- Larkin M.A., Blackshields G., Brown N.P., Chenna R., McGettigan P.A., McWilliam H., Valentin F., Wallace I.M., Wilm A., Lopez R., et al. Clustal W and Clustal X version 2.0. // Bioinformatics. 2007. V. 23. № 21. P. 2947−2948.
- Schneider T.D., Stephens R.M. Sequence logos: a new way to display consensus sequences. //Nucleic Acids Res. 1990. V. 18. № 20. P. 6097−6100.
- Crooks G.E., Hon G., Chandonia J.M., Brenner S.E. WebLogo: a sequence logo generator. // Genome Res. 2004. V. 14. № 6. P. 1188−1190.
- Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. // Electrophoresis. 1997. V. 18. № 15. P. 2714−2723.
- DeLano W.L. The PyMOL Molecular Graphics System. 2007, DeLano Scientific LLC, Palo Alto, CA, USA.
- Акимкина T.B., Носовская E.A., Костров С. В. Клонирование и экспрессия гена нейтральной протеиназы В. cereus в клетках В. subtilis. // Мол биол. 1992. Т. 26. № 2. Р. 418−423.
- Erlanger B.F., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. //Arch Biochem Biophys. 1961. V. 95. P. 271−278.
- Sarkar G., Sommer S.S. The «megaprimer» method of site-directed mutagenesis. // Biotechniques. 1990. V. 8. № 4. P. 404−407.
- Заболотская M.B., Носовская E.A., Каплун M.A., Цаплина И. А., Акимкина Т. В. Новая термостабильная протеиназа на Thermoactinomyces sp. 27а. Клонирование и экспрессия гена. // Мол ген микробиол вирусол. 2001. № 1. Р. 32−34.
- Feder J. A spectrophotometry assay for neutral protease. // Biochem Biophys Res Commun. 1968. V. 32. № 2. P. 326−332.
- Inouye K. Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. // J Biochem. 1992. V. 112. № 3. P. 335−340.
- Tsu C.A., Perona J.J., Schellenberger V., Turck C.W., Craik C.S. The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites. // J Biol Chem. 1994. V. 269. № 30. P. 19 565−19 572.
- Журавская Н.К., Алехина JT.T., Отряшенкова JI.M. Исследование и контроль качества мяса и мясопродуктов. М. Агропромиздат, 1985. 295 р.
- ЛюблинскаяЛ.А., ВагановаТ.И., ПасхинаТ.С., СтепановВ.М.2,4-Динитрофенил-производные пептидов субстраты нового типа для определения активности протеолитических ферментов. Определение активности карбоксипептпдаз. // Биохимия. 1973. Т. 38. № 4. Р. 790−795.
- Честухина Г. Г., Загнитько О. П., Ревина Л. П., Клепикова Ф. С., Степанов В. М. Внеклеточные сериновые протеазы подвидов Bacillus thutingiensis эволюционируют существенно медленнее сответствующих 8-эндотоксинов. //Биохимия. 1985. Т. 50. № 10. Р. 1724−1732.
- Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. // J Appl Crystallogr. 1993. V. 26. № 6. P. 795−800.
- Long F., Vagin A.A., Young P., Murshudov G.N. BALBES: a molecular-replacement pipeline. // Acta Crystallogr, Sect D: Biol Crystallogr. 2008. V. 64 (Pt 1). P. 125−132.
- Vagin A., Teplyakov A. MOLREP: an Automated Program for Molecular Replacement. //J Appl Crystallogr. 1997. V. 30. № 6. P. 1022−1025.
- The CCP4 suite: programs for protein crystallography. // Acta Crystallogr, Sect D: Biol Crystallogr. 1994. V. 50 (Pt 5). P. 760−763.
- Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of Macromolecular Structures by the Maximum-Likelihood Method. // Acta Crystallogr, Sect D: Biol Crystallogr. 1997. V. 53. № 3. P. 240−255.
- Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. // Acta Crystallogr, Sect D: Biol Crystallogr. 2004. V. 60 (Pt 12, Pt 1). P. 2126−2132.
- Diederichs K., Karplus P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. //Nat. Struct. Biol. 1997. V. 4. № 4. P. 269−275.
- Pivovarova A.V., Khaitlina S.Y., Levitsky D.I. Specific cleavage of the DNase-I binding loop dramatically decreases the thermal stability of actin. // FEBS J. 2010. V. 277. № 18. P. 3812−3822.
- Itzhaki R.F., Gill D.M. A micro-biuret method for estimating proteins. // Anal Biochem. 1964. V. 9. P. 401−410.
- Kouyama Т., Mihashi K. Fluorimetry study of N-(l-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. // Eur J Biochem. 1981. V. 114. № 1. P. 33−38.
- Kodama Т., Fukui K., Kometani K. The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. // J Biochem. 1986. V. 99. № 5. P. 1465−1472.
- Беляева E.B., Руденская Г. Н., Степанов B.M., Дегтева Г. К. Выделение и свойства внеклеточной протеиназы золотистого стафилококка. // Прикл биохим микробиол. 1984. Т. 20. № 3. Р. 363−368.
- Гасанов E.B., Романова Д. В., Громова Т. Ю., Демидюк И. В. Эффект делеции З'-некодирующей области гена глутамилэндопептидазы Bacillus intermedius на продукцию активного белка клетками Bacillus subtilis. // Мол ген микробиол вирусол. 2007. № 2. Р. 31−32.
- Jana S., Deb J.K. Strategies for efficient production of heterologous proteins in Escherichia coli. //Appl Microbiol Biotechnol. 2005. V. 67. № 3. P. 289−298.
- Nudler E., Gottesman M.E. Transcription termination and anti-termination in E. coli. // Genes to Cells. 2002. V. 7. № 8. P. 755−768.
- Thornberry N.A., Molineaux S.M. Interleukin-1 beta converting enzyme: a novel cysteine protease required for IL-1 beta production and implicated in programmed cell death. // Protein Sci. 1995. V. 4. № 1. P. 3−12.
- Демидюк И.В., Костров С. В. Особенности функциональной организации глутамилэндопептидаз. //Мол биол. 1999. Т. 33. № 1. Р. 100−105.
- Demidyuk I.V., Romanova D.V., Nosovskaya Е.А., Chestukhina G.G., Kuranova I.P., Kostrov S.V. Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius. // Protein Eng Des Sel. 2004. V. 17. № 5. P. 411−416.
- Lesk A.M., Fordham W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. // J Mol Biol. 1996. V. 258. № 3. P. 501−537.
- Power S.D., Adams R.M., Wells J.A. Secretion and autoproteolytic maturation of subtilisin. // Proc Natl Acad Sci USA. 1986. V. 83. № 10. P. 3096−3100.
- Marie-Claire C., Roques B. P, Beaumont A. Intramolecular processing of prothermolysin. // J Biol Chem. 1998. V. 273. № 10. P. 5697−5701.
- Sloma A., Rufo G.A., Jr., Rudolph C.F., Sullivan B.J., Theriault K.A., Pero J. Bacillopeptidase F of Bacillus subtilis: purification of the protein and cloning of the gene. // J Bacteriol. 1990. V. 172. № 3. P. 1470−1477.
- Wu X.C., Nathoo S., Pang A.S., Carne Т., Wong S.L. Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis. // J Biol Chem. 1990. V. 265. № 12. P. 6845−6850.
- Hageman J.H. Bacillopeptidase F, in Handbook of Proteolytic Enzymes, 2 edn, A.J. Barrett, Editor. 2004, London, p. 1795−1796.
- Ikemura H., Inouye M. In vitro processing of pro-subtilisin produced in Escherichia coli. // J Biol Chem. 1988. V. 263. № 26. P. 12 959−12 963.
- Suh Y., Benedik M.J. Production of active Serratia marcescens metalloprotease from Escherichia coli by alpha-hemolysin HlyB and HlyD. // J Bacteriol. 1992. V. 174. № 7. P. 2361−2366.
- Nishiya Y., Imanaka T. Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene. // J Bacteriol. 1990. V. 172. № 9. P. 4861−4869.
- Kuhn S., Fortnagel P. Molecular cloning and nucleotide sequence of the gene encoding a calcium-dependent exoproteinase from Bacillus megaterium ATCC 14 581.// J Gen Microbiol. 1993. V. 139. № 1. P. 39−47.
- Аваков А.С., Болотин А. П., Сорокин A.B. Структура гена металлопротеиназы Bacillus brevis. Молекулярная биология. // Мол биол. 1990. Т. 24. № 5. Р. 13 631 372.
- Takekawa S., Uozumi N., Tsukagoshi N., Udaka S. Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa. // J Bacteriol. 1991. V. 173. № 21. P. 6820−6825.
- Tran L., Wu X.C., Wong S.L. Cloning and expression of a novel protease gene encoding an extracellular neutral protease from Bacillus subtilis. // J Bacteriol. 1991. V. 173. № 20. P. 6364−6372.
- Inouye K., Lee S.B., Tonomura B. Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. // Biochem J. 1996. V. 315 (Pt 1). P. 133−138.
- Костенко Ю.Г., Спицина Д. Н., Батаева Д. С., Костров С. В., Носовская Е. А. Штамм Serratia proteamaculans 94 продуцент коллагеназы. // Патент Российской Федерации № 2 175 350. 2001.
- Kyostio S.R., Cramer C.L., Lacy G.H. Erwinia carotovora subsp. carotovora extracellular protease: characterization and nucleotide sequence of the gene. // J Bacteriol. 1991. V. 173. № 20. P. 6537−6546.
- Kwon Y.T., Lee H.H., Rho H.M. Cloning, sequencing, and expression of a minor protease-encodinggene from Serratiamarcescens ATCC21074. //Gene. 1993. V. 125. № l. P 75−80.
- Frigerio F., Margarit I., Nogarotto R., Grandi G., Vriend G., Hardy F., Veltman O.R., Venema G., Eijsink V.G. Model building of a thermolysin-like protease by mutagenesis. //Protein Eng. 1997. V. 10. № 3. P. 223−230.
- Toma S., Campagnoli S., Margarit I., Gianna R., Grandi G., Bolognesi M., De Filippis V., Fontana A. Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease. //Biochemistry. 1991. V. 30. № 1. R 97−106.
- Vriend G., Eijsink V. Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases. // J Comput Aided Mol Des. 1993. V. 7. № 4. P. 367−396.
- Dahlquist F.W., Long J.W., Bigbee W.L. Role of Calcium in the thermal stability of thermolysin. //Biochemistry. 1976. V. 15. № 5. P. 1103−1111.
- Veltman O.R., Vriend G., van den Burg В., Hardy F., Venema G., Eijsink V.G. Engineering thermolysin-like proteases whose stability is largely independent of calcium. // FEBS Lett. 1997. V. 405. № 2. P. 241−244.
- Veltman O.R., Vriend G., Berendsen H.J., van den Burg В., Venema G., Eijsink V.G. A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases. //Biochemistry. 1998. V. 37. № 15. P. 5312−5319.
- Matthews B.W. Structural basis of the action of thermolysin and related zinc peptidases. //Acc Chem Res. 1988. V. 21. P. 333−340.
- Argos P., Garavito R.M., Eventoff W., Rossmann M.G., Branden C.I. Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases. //J Mol Biol. 1978. V. 126. № 2. P. 141−158.
- Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. // FEBS Lett. 1989. V. 242. № 2. P. 211−214.
- Demidyuk I.V., Shubin A.V., Gasanov E.V., Kostrov S.V. Propeptides as modulators of functional activity of proteases. // BioMolecular Concepts. 2010. V. 1. № 3−4. P. 305−322.
- Miyoshi S., Wakae H., Tomochika K., Shinoda S. Functional domains of a zinc metalloprotease from Vibrio vulnificus. // J Bacteriol. 1997. V. 179. № 23. P. 7606−7609.
- Miyoshi S., Kawata K., Tomochika K., Shinoda S., Yamamoto S. The C-terminal domain promotes the hemorrhagic damage caused by Vibrio vulnificus metalloprotease. //Toxicon. 2001. V. 39. № 12. P. 1883−1886.
- Miyamoto K., Nukui E., Hirose M., Nagai F., Sato T., Inamori Y., Tsujibo H. A metalloprotease (Mprlll) involved in the chitinolytic system of a marine bacterium, Alteromonas sp. strain 0−7. // Appl Environ Microbiol. 2002. V. 68. № 11. P. 5563−5570.
- Bateman A., Coin L., Durbin R., Finn R.D., Hollich V., Griffiths-Jones S., Khanna A., Marshall M., Moxon S., Sonnhammer E.L., et al. The Pfam protein families database. //Nucleic Acids Res. 2004. V. 32. Database issue. P. D138−141.
- Yeats C., Rawlings N.D., Bateman A. The PepSY domain: a regulator of peptidase activity in the microbial environment? // Trends Biochem Sci. 2004. V. 29. № 4. P. 169−172.
- Braun P., Ockhuijsen C., Eppens E., Koster M., Bitter W., Tommassen J. Maturation ofPseudomonas aeruginosa elastase. Formation of the disulfide bonds. // J Biol Chem.2001. V. 276. № 28. P. 26 030−26 035.
- Hase C.C., Finkelstein R.A. Comparison of the Vibrio cholerae hemagglutinin/ protease and the Pseudomonas aeruginosa elastase. // Infect Immun. 1990. V. 58. № 12. P. 4011−4015.
- Norqvist A., Norrman B., Wolf-Watz H. Identification and characterization of a zinc metalloprotease associated with invasion by the fish pathogen Vibrio anguillarum. // Infect Immun. 1990. V. 58. № 11. P. 3731−3736.
- Oda K., Okayama K., Okutomi K., Shimada M., Sato R., Takahashi S. A novel alcohol resistant metalloproteinase, vimelysin, from vibrio sp. T1800: purification and characterization. // Biosci Biotechnol Biochem. 1996. V. 60. № 3. P. 463−467.
- Kato J.Y., Suzuki A., Yamazaki H., Ohnishi Y., Horinouchi S. Control by A-factor of a metalloendopeptidase gene involved in aerial mycelium formation in Streptomyces griseus. // J Bacteriol. 2002. V. 184. № 21. P. 6016−6025.
- Miyoshi N., Shimizu C., Miyoshi S., Shinoda S. Purification and characterization of Vibrio vulnificus protease. // Microbiol Immunol. 1987. V. 31. № 1. P. 13−25.
- Chuang Y.C., Chang T.M., Chang M.C. Cloning and characterization of the gene (empV) encoding extracellular metalloprotease from Vibrio vulnificus. // Gene. 1997. V. 189. № 2. P. 163−168.
- David V.A., Deutch A.H., Sloma A., Pawlyk D., Ally A., Durham D.R. Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. // Gene. 1992. V. 112. № 1. P. 107−112.
- Teo J.W., Zhang L.H., Poh C.L. Cloning and characterization of a metalloprotease from Vibrio harveyi strain AP6. // Gene. 2003. V. 303. P. 147−156.
- Behmlander R.M., Dworkin M. Biochemical and structural analyses of the extracellular matrix fibrils of Myxococcus xanthus. // J Bacteriol. 1994. V. 176. № 20. P. 6295−6303.
- Toyoshima T., Matsushita O., Minami J., Nishi N., Okabe A., Itano T. Collagen-binding domain of a Clostridium histolyticum collagenase exhibits a broad substrate spectrum both in vitro and in vivo. // Connect Tissue Res. 2001. V. 42. № 4. P. 281−290.
- Matsushita O., Koide T., Kobayashi R., Nagata K., Okabe A. Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase. // J Biol Chem. 2001. V. 276. № 12. P. 8761−8770.
- Creemers J.W., Siezen R.J., Roebroek A.J., Ayoubi T.A., Huylebroeck D., Van de Ven W.J. Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis. // J Biol Chem. 1993. V. 268. № 29. P. 21 826−21 834.
- Gluschankof P., Fuller R.S. A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal maturation of pro-Kex2 protease. // EMBO J. 1994. V. 13. № 10. P. 2280−2288.
- Zhou A., Martin S., Lipkind G., LaMendola J., Steiner D.F. Regulatory roles of the P domain of the subtilisin-like prohormone convertases. // J Biol Chem. 1998. V. 273. № 18. P. 11 107−11 114.
- Zhu X., Muller L., Mains R.E., Lindberg I. Structural elements of PC2 required for interaction with its helper protein 7B2. // J Biol Chem. 1998. V. 273. № 2. P. 1158−1164.
- Stepanov V.M., Rudenskaya G.N. Proteinase affinity chromatography on bacitracin-Sepharose. // J Appl Biochem. 1983. V. 5. № 6. P. 420−428.
- Held K.G., LaRock C.N., D’Argenio D.A., Berg C.A., Collins C.M. Ametalloprotease secreted by the insect pathogen Photorhabdus luminescens induces melanization. // Appl Environ Microbiol. 2007. V. 73. № 23. P. 7622−7628.
- GromovaT.Y., Demidyukl.V., KozlovskiyV.I., KuranovaI.P., Kostrov S.V. Processing of protealysin precursor. // Biochimie. 2009. V. 91. № 5. P. 639−645.
- Matthews B.W. Solvent content of protein crystals. // J. Mol. Biol. 1968. V. 33. № 2. P. 491−497.
- Kantardjieff K.A., Rupp B. Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. // Protein Sci. 2003. V. 12. № 9. P. 1865−1871.
- Matthews B.W., Jansonius J.N., Colman P.M., Schoenborn B.P., Dupourque D. Three-dimensional structure of thermolysin. // Nature New Biol. 1972. V. 238. P. 37−41.
- Stark W., Pauptit R.A., Wilson K.S., Jansonius J.N. The structure of neutral protease from Bacillus cereus at 0.2-nm resolution. // Eur J Biochem. 1992. V. 207. № 2. P. 781−791.
- Thayer M.M., Flaherty K.M., McKay D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. // J Biol Chem. 1991. V. 266. № 5. P. 2864−2871.
- Roche R.S., Voordouw G. The structural and functional roles of metal ions in thermolysin. // CRC Crit Rev Biochem. 1978. V. 5. № 1. P. 1−23.
- Corbett R.J., Roche R.S. The unfolding mechanism of thermolysin. // Biopolymers. 1983. V. 22. № l.p. 101−105.
- Khaitlina S., Smirnova T.D., Usmanova A.M. Limited proteolysis of actin by a specific bacterial protease. // FEBS Lett. 1988. V. 228. № 1. P. 172−174.
- Bozhokina E., Khaitlina S., Adam T. Grimelysin, a novel metalloprotease from Serratia grimesii, is similar to ECP32. // Biochem Biophys Res Commun. 2008. V. 367. № 4. P. 888−892.
- Цаплина O.A., Ефремова Т. Н., Кевер JI.B., Комиссарчик Я. Ю., Демидюк И. В., Костров С. В., Хайтлина С. Ю. Выявление актиназной активности протеализина. // Биохимия. 2009. Т. 74. № 6. Р. 797−804.
- McKay D.B., Thayer М.М., Flaherty K.M., Pley H., Benvegnu D. Crystallographic structures of the elastase of Pseudomonas aeruginosa. // Matrix Suppl. 1992. V. 1. P. 112−115.
- Hausrath A.C., Matthews B.W. Thermolysin in the absence of substrate has an open conformation. // Acta Crystallogr, Sect D: Biol Crystallogr. 2002. V. 58 (Pt 6, Pt 2). P. 1002−1007.
- Hangauer D.G., Monzingo A.F., Matthews B.W. An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides. // Biochemistry. 1984. V. 23. № 24. P. 5730−5741.
- Feder J. Studies on the specificity of Bacillus subtilis neutral protease with synthetic substrates. // Biochemistry. 1967. V. 6. № 7. P. 2088−2093.
- Feder J., Schuck J.M. Studies on the Bacillus subtilis neutral-protease- and Bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substrates. // Biochemistry. 1970. V. 9. № 14. P. 2784−2791.
- Tsaplina O., Efremova Т., Demidyuk I., Khaitlina S. Filamentous actin is a substrate for protealysin, a metalloprotease of invasive Serratia proteamaculans. // FEBS J. 2012. V. 279. № 2. P. 264−274.
- Cabral C.M., Cherqui A., Pereira A., SimoesN. Purification and characterization of two distinct metalloproteases secreted by the entomopathogenic bacterium Photorhabdus sp. strain Az29. //Appl Environ Microbiol. 2004. V. 70. № 7. P. 3831−3838.
- Izore T., Job V., Dessen A. Biogenesis, regulation, and targeting of the type III secretion system. // Structure. 2011. V. 19. № 5. P. 603−612.
- Cascales E., Cambillau C. Structural biology of type VI secretion systems. // Philos Trans R Soc Lond B Biol Sei. 2012. V. 367. № 1592. P. 1102−1111.
- Schultz D.R., Miller K.D. Elastase of Pseudomonas aeruginosa: inactivation of complement components and complement-derived chemotactic and phagocytic factors. // Infect Immun. 1974. V. 10. № 1. P. 128−135.
- Mariencheck W.I., Alcorn J.F., Palmer S.M., Wright J.R. Pseudomonas aeruginosa elastase degrades surfactant proteins A and D. // Am J Respir Cell Mol Biol. 2003. V. 28. № 4. P. 528−537.
- Kuang Z., Hao Y., Walling B.E., Jeffries J.L., Ohman D.E., Lau G.W. Pseudomonas aeruginosa Elastase Provides an Escape from Phagocytosis by Degrading the Pulmonary Surfactant Protein-A. // PLoS One. 2011. V. 6. № 11. P. e27091.
- Schmidtchen A., Frick I.M., Andersson E., Tapper H., Bjorck L. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. // Mol Microbiol. 2002. V. 46. № 1. P. 157−168.
- Diebel L.N., Liberati D.M., Amin P.B., Diglio C. A. Cleavage of SIgAby gram negative respiratory pathogens enhance neutrophil inflammatory potential. // J Trauma. 2009. V. 66. № 5. P. 1336−1342.
- Holder I.A., Wheeler R. Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: elastase, an IgG protease. // Can J Microbiol. 1984. V. 30. № 9. P. 1118−1124.
- Mintz C.S., Miller R.D., Gutgsell N.S., Malek T. Legionella pneumophila protease inactivates interleukin-2 and cleaves CD4 on human T cells. // Infect Immun. 1993. V. 61. № 8. P. 3416−3421.
- Grimont F., Grimont P. The Genus Serratia, in The Prokaryotes, M. Dworkin, Editor. 2006, New York. p. 219−244.
- Jackson T.A., Boucias D.G., Thaler J.O. Pathobiology of amber disease, caused by Serratia spp., in the New Zealand grass grub, Costelytra zealandica. // J Invertebr Pathol. 2001. V. 78. № 4. P. 232−243.
- Bollet C., Grimont P., Gainnier M., Geissler A., Sainty J.M., De Micco P. Fatal pneumonia due to Serratia proteamaculans subsp. quinovora. // J Clin Microbiol. 1993. V. 31. № 2. P. 444−445.
- Усманова A.M., Хайтлина С. Ю. Протеаза из штамма бактерий Е2, специфически расщепляющая актин. // Биохимия. 1989. Т. 54. № 8. Р. 1308−1314.
- Ефремова Т.Н., Эндер H.A., Комиссарчик Я. Ю., Хайтлина С. Ю. Реорганизация актиновых микрофиламентов в клетках Нер-2 в результате инвазии бактерий Escherichia coli А2. // Цитология. 1998. Т. 40. № 6. Р. 524−528.
- Efremova Т., Ender N., Brudnaja М., Komissarchik Y., Khaitlina S. Specific invasion of transformed cells by Escherichia coli A2 strain. // Cell Biol Int. 2001. V. 25. № 6. P. 557−561.
- Khaitlina S., Collins J.H., Kuznetsova I.M., Pershina V.P., Synakevich I.G., Turoverov K.K., Usmanova A.M. Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. // FEBS Lett. 1991. V. 279. № 1. P. 49−51.
- Khaitlina S.Y., Strzelecka-Golaszewska H. Role of the DNase-I-binding loop in dynamic properties of actin filament. // Biophys J. 2002. V. 82. № 1 (Pt 1). P. 321−334.
- Carlier M.F., Pantaloni D., Korn E.D. Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state. // J Biol Chem. 1984. V. 259. № 16. P. 9983−9986.
- Dai S., Sarmiere P.D., Wiggan O., Bamburg J.R., Zhou D. Efficient Salmonella entry requires activity cycles of host ADF and cofilin. // Cell Microbiol. 2004. V. 6. № 5. P. 459−471.
- Cossart P., Sansonetti P.J. Bacterial invasion: the paradigms of enteroinvasive pathogens. // Science. 2004. V. 304. № 5668. P. 242−248.1