Разработка новых подходов к изучению «слабого» связывания миозина с актином
Диссертация
Связывание миозиновой головки с актином протекает в несколько этапов. «Сильное» связывание, характерное для этих белков в отсутствие нуклеотида, резко ослабляется при связывании миозиновой головкой молекулы АТР. Миозиновая головка гидролизует АТР на ADP и Pj, что сопровождается значительными конформационными изменениями головки. В этом состоянии миозиновая головка снова способна связаться… Читать ещё >
Содержание
- Список использованных
- Обзор литературы
- 1. 1. Структура и основные свойства актина
- 1. 1. 1. Биологическая характеристика актина
- 1. 1. 2. Функциональные свойства актина. Полимеризация
- 1. 1. 3. Структура молекулы актина 1.1.3.1. Участки связывания лигандов
- 1. 1. Структура и основные свойства актина
- 1. 2. Структура и основные свойства тропомиозина 1.3 Структура и основные свойства миозина
- 1. 3. 1. Строение молекулы миозина
- 1. 3. 2. АТРазная активность миозина
- 1. 3. 3. Стабильные аналоги интермедиатов 81**-АВР-Р^ и 81*-АТР
- 1. 4. Взаимодействие миозина с актином
- 1. 4. 1. Молекулярный механизм подвижности
- 1. 4. 2. «Слабое» и «сильное» связывание миозина с актином
- 1. 4. 3. Регуляция сокращения
- 1. 5. Применение метода дифференциальной сканирующей калориметрии для структурных исследований мышечных белков
- 2. 1. Получение препаратов белков
- 2. 1. 1. Выделение миозина из скелетных мышц кролика
- 2. 1. 2. Получение субфрагмента 1 (S1) миозина из скелетных мышц кролика
- 2. 1. 3. Выделение актина из скелетных мышц кролика
- 2. 1. 4. Приготовление препарата гладкомышечного тропомиозина
- 2. 1. 5. Разделение гладкомышечного тропомиозина на изоформы
- 2. 2. Используемые биохимические методы
- 2. 2. 1. Формирование стабильных тройных комплексов Sic ADP и аналогами
- 2. 2. 2. Определение АТРазной активности миозина
- 2. 2. 3. Пиреновая модификация актина
- 2. 2. 4. Измерение концентрации белка микробиуретовым методом
- 2. 3. Использованные методы исследования
- 2. 3. 1. Кинетические методы исследования
- 2. 3. 2. Исследования тепловой денатурации белков методом дифференциальной сканирующей калориметрии (ДСК)
- 2. 3. 3. Исследование температурных зависимостей диссоциации комплекса F-актина с тропомиозином по изменению интенсивности светорассеяния
- 3. 1. Кинетические исследования «слабого» связывания головок миозина с F-акгином
- 3. 1. 1. Исследования скорости образования тройных комплексов 81- АБР-АШ4″ и 81-А1)Р-ВеРх в отсутствие и присутствии Б-актина
- 3. 1. 2. Доказательство «слабого» связывания комплексов 81-АБР-ВеРх и 81-АБР-А1Р4″ с Р-актином
- 3. 1. 3. Сравнительный кинетический анализ «слабого» связывания с Р-актином тройных комплексов
- 3. 2. 1. Тепловая денатурация комплекса ТМ — Р-актин
- 3. 2. 2. Тепловая денатурация связанного с актином ТМ при различных молярных отношениях ТМ: актин
- 3. 2. 3. Влияние разведения комплекса ТМ — Р-актин на тепловую денатурацию связанного с актином ТМ
- 3. 2. 4. Исследование тепловой денатурации гомодимеров ТМ в комплексе с Р-актином
- 3. 2. 5. Исследование процесса тепловой денатурации комплекса Р-актин — ТМ в присутствии кальдесмона
- 3. 2. 6. Изучение методом ДСК комплекса Р-актин — ТМ в присутствии
Список литературы
- Веденкина Н. С., Калиниченко Л. П., Пермяков Е. А. Влияние фаллоидина на стабильность Б- и в-актина. Молек. биология, 1995, т. 29, С. 597−602.
- Левицкий Д. И., Хайтлина С. Ю., Гусев Н. Б. «Белки актомиозиновой системы подвижности». В книге Белки и пептиды, Т. 1, 1995, (под ред. Иванова БТ, Липкина ВМ), Наука, Москва, с. 249−293.
- Левицкий Д. И., Бобков А. А., Голицына Н. Л., Николаева О. П., Павлов Д. А, Поглазов Б. Ф. Калориметрические исследования стабильных комплексов субфрагмента 1 миозина с аналогами аденозинтрифосфата и фосфата. Биофизика, 1996, т. 41, № 1, С. 6472.
- Левицкий Д. И., Николаева О. П., Орлов В. Н., Павлов Д. А., Пономарев М. А., Росткова Е. В. Дифференциальная сканирующая калориметрия миозина и актина. Биохимия, 1998, т. 63, № 3, С. 391−394.
- Поглазов Б. Ф., Билуши В., Баев А. А. О сульфгидрильных группах миозиновой аденозинтрифосфатазы. Биохимия, 1958, т. 23, № 2, С. 269−284.
- Anson, M., Geeves, M. A., Kurzawa, S. E., Manstein, D. J: Myosin motors with artificial lever arms. EMBOJ., 1996- v. 15, p. 6069−6074.
- Arner, A., Malmqvist, U: Cross-bridge cycling in smooth muscle: a short review. Acta Physiol. Scand. 1998- v. 164, p. 363−372
- Ayscough, K. R: In vivo functions of actin-binding proteins. Curr.Opin.Cell Biol., 1998- v. 10, p.102−111
- Bertazzon, A., Tian, G. H., Lamblin, A., Tsong, T. Y: Enthalpic and entropic contributions to actin stability: calorimetry, circular dichroism, and fluorescence study and effects of calcium. Biochemistry, 1990- v. 29, p. 291−298
- Block, S. M: Fifty ways to love your lever: myosin motors. Cell, 1996- v. 87, p. 151 157
- Boudker, O., Todd, M.J., Freire, E: The structural stability of the co-chaperonin GroES. J. Mol. Biol., 1997- v. 272, p. 770−779
- Carlier, M.F., Pantaloni, D., Korn, E. D: The mechanisms of ATP hydrolysisaccompanying the polymerization of Mg- actin and Ca-actin. J. Biol. Chem., 1987- v. 262, p. 3052−3059
- Carlier, M. F: Actin polymerization and ATP hydrolysis. Adv. Biophys., 1990- v. 26, p. 51−73
- Carlier, M.F., Didry, D: Interaction of myosin sub fragment-1 with F- and G-actin in equilibrium. Biochem. Biophys. Res. Commun., 1992- v. 183, p. 970−974
- Carlier, M. F: Control of actin dynamics. Curr. Opin. Cell Biol., 1998- v. 10, p. 45−51
- Chalovich, J. M., Chock, P. B., Eisenberg, E: Mechanism of action of troponin.tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin. J.Biol. Chem., 1981- v. 256, p. 575−578
- Chalovich, J.M., Greene, L.E., Eisenberg, E: Crosslinked myosin subfragment 1: a stable analogue of the subfragment- 1 ATP complex. Proc. Natl. A cad. Sci. U.S.A., 1983- v. 80, p. 4909−4913
- Cho, Y.J., Hitchcock-DeGregori, S. E: Relationship between alternatively splicedexons and functional domains in tropomyosin. Proc.Natl.Acad.Sci. U.S.A., 1991- v. 88, p. 10 153−10 157
- Conibear, P. B., Geeves, M. A: Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin. Biophys.J., 1998- v. 75, p. 926−937
- Cossart, P: Actin-based bacterial motility. Curr.Opin.CellBiol, 1995- v. 7, p. 94−101
- Cowin, P., Burke, B: Cytoskeleton-membrane interactions. Curr.Opin.Cell Biol., 1996- v. 8, p. 56−65
- Cramer, L. P., Mitchison, T. J., Theriot, J. A: Actin-dependent motile forces and cell motility. Curr.Opin.Cell Biol., 1994- v. 6, p.82−86
- Criddle, A. H., Geeves, M. A., Jeffries, T: The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem.J., 1985- v. 232, p. 343 349
- DalleDonne, I., Milzani, A., Colombo, R: Actin assembly by cadmium ions. Biochim.Biophys.Acta 1997- v. 1357, p. 5−17
- DalleDonne, I., Milzani, A., Ciapparelli, C., Comazzi, M., Gioria, M. R., Colombo, R: The assembly of Ni2±actin: some peculiarities. Biochim.Biophys.Acta, 1999- v. 1426, p. 32−42
- Drubin, D. G., Jones, H. D., Wertman, K. F: Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin- binding site. Mol.Biol. Cell, 1993- v. 4, p. 1277−1294
- Duke, T. A. J: Molecular model of muscle contraction. Proc.Natl.Acad.Sci. U.S.A., 1999- v. 96, p. 2770−2775
- Eisenberg, E., Kielley, W. W: Troponin-tropomyosin complex. Columnchromatographic separation and activity of the three, active troponin components with and without tropomyosin present. J.Biol. Chem., 1974- v. 249, p. 4742−4748
- Eisenberg, E., Hill, T. L: Muscle contraction and free energy transduction in biological systems. Science, 1985- v. 227, p. 999−1006
- Faulstich, H., Zobeley, S., Heintz, D., Drewes, G: Probing the phalloidin binding site of actin. FEBSLett., 1993- v. 8, p. 218−222
- Ferraz, C., Derancourt, J., Sri, W.J., Liautard, J. P: Structural analysis of humanskeletal beta-tropomyosin produced in E. coli. Biochimie, 1989- v. 71, p. 307−312
- Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., Rayment, I: Structural studies of myosin: nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys.J., 1995- v. 68, p. 19S-26S
- Fisher, A. J., Smith, C. A., Thoden, J. B" Smith, R., Sutoh, K., Holden, H. M.,
- Rayment I: X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP. BeFx and MgADP. AlF4-.
- Biochemistry, 1995- v. 34, p. 8960−8972
- Freire, E: Differential scanning calorimetry. Methods Mol.Biol., 1995- v. 40, p. 191 218
- Friedman, A. L., Geeves, M. A., Manstein, D. J., Spudich, J. A: Kineticcharacterization of myosin head fragments with long-lived myosin. ATP states. Biochemistry 1998- v. 37, p. 9679−9687
- Furch, M., Geeves, M.A., Manstein, D. J: Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry, 1998- v. 37, p. 6317−6326
- Geeves, M. A: The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem.J., 1991- v. 274 (Pt 1), p. 1−14
- Geeves, M. A., Conibear, P. B: The role of three-state docking of myosin SI with actin in force generation. Biophys.J., 1995- v. 68, p. 194S-199S
- Goldman, Y. E: Wag the tail: structural dynamics of actomyosin. Cell, 1998- v. 93, p. 1−4
- Gollub. J., Cremo. C. R., Cooke. R.: ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin see comments. Nat.Struct.Biol., 1996- v. 3, p. 796−802
- Goodson, H. V., Warrick, H. M., Spudich, J. A: Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics. J.Mol.Biol., 1999- v. 287, p. 173−185
- Gopal, D., Burke, M: Formation of stable inhibitory complexes of myosinsubfragment 1 using fluoroscandium anions. J.Biol.Chem., 1995- v. 270, p. 19 282−19 286
- Graceffa, P: Movement of smooth muscle tropomyosin by myosin heads. Biochemistry, 1999- v. 38, p. 11 984−11 992
- Gulick, A. M., Bauer, C. B., Thoden, J.B., Rayment, I: X-ray structures of the
- MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry, 1997- v. 36, p. 11 619−11 628
- Gunning, P., Weinberger, R., Jeffrey, P: Actin and tropomyosin isoforms in morphogenesis. Anat.Embryol.(Berl), 1997- v. 195, p. 311−315
- Hammell, R. L., Hitchcock-DeGregori, S. E: Mapping the functional domains within the carboxyl terminus of alpha- tropomyosin encoded by the alternatively spliced ninth exon. J.Biol.Chem., 1996- v. 271, p. 4236−4242
- Heintz, D., Faulstich, H: Cross-link between cys 374 and cys 10 of actin abolishes polymerizability and allows study of the properties of the «F-actin monomer». Biochemistry, 1996- v. 35, p. 258−265
- Henry, G. D., Maruta, S., Ikebe, M., Sykes, B. D: Observation of multiple myosin subfragment 1-ADP-fluoroberyllate complexes by 19 °F NMR spectroscopy. Biochemistry, 1993- v. 32, p. 10 451−10 456
- Hild, G., Nyitrai, M., Belagyi, J., Somogyi, B: The influence of divalent cations on the dynamic properties of actin filaments: a spectroscopic study. Biophys.J., 1998- v. 75, p. 3015−3022
- Holmes, K. C., Popp, D., Gebhard, W., Kabsch, W: Atomic model of the actin filament see comments. Nature, 1990- v. 347, p. 44−49
- Holmes, K. C: The actomyosin interaction and its control by tropomyosin. Biophys.J., 1995- v. 68, p. 2S-5S
- Holmes, K. C: Muscle proteins-their actions and interactions. Curr.Opin.Struct.Biol, 1996- 6: p. 781−789
- Holmes K. C.: The swinging lever-arm hypothesis of muscle contraction. Curr.Biol. 1997- v. 7, p. R112-R118
- Holmes, K. C: A molecular model for muscle contraction. Acta Crystallogr.A., 1998- v. 54, p. 789−797
- Holtzer, M. E., Breiner, T., Holtzer, A.: Hetero-alpha-helical, two-chain, coiled coils: alpha beta hybrid tropomyosin. Biopolymers 1984- v. 23, p. 1811−1833
- Holtzer, M. E., Crimmins, D. L., Holtzer, A: Structural stability of short subsequences of the tropomyosin chain. Biopolymers, 1995- v. 35, p. 125−136
- Holtzer, M. E., Holtzer, A: The use of spectral decomposition via the convexconstraint algorithm in interpreting the CD-observed unfolding transitions of coiled coils. Biopolymers, 1995- v. 36, p. 365−379
- Hori, K., Morita, F: Actin-actin contact: inhibition of actin-polymerization bysubdomain 4 peptide fragments. J.Biochem.(Tokyo.), 1992- v. 112, p. 401 408
- Huxley, H. E., Kress, M: Crossbridge behaviour during muscle contraction. J. Muscle Res. Cell Motil., 1985- v. 6, p. 153−161
- Jancso, A., Graceffa, P: Smooth muscle tropomyosin coiled-coil dimers. Subunitcomposition, assembly, and end-to-end interaction. J.Biol.Chem., 1991- v. 266, p. 5891−5897
- Johnson, C. M., Fersht, A. R: Protein stability as a function of denaturantconcentration: ther thermal stability of barnase in the presence of urea. Biochemistry, 1995- v. 34, p. 6795−6804
- Jontes, J. D., Wilson-Kubalek, E. M., Milligan, R. A: A 32 degree tail swing in brush border myosin I on ADP release. Nature, 1995- v. 378, p. 751−753
- Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., Holmes, K. C: Atomic structure of the actin: DNase I complex. Nature, 1990- v. 347, p. 37−44
- Kabsch, W., Holmes, K. C: The actin fold. FASEBJ., 1995- v. 9, p. 167−174
- Katoh, T., Morita, F: Mapping myosin-binding sites on actin probed by peptides that inhibit actomyosin interaction. J.Biochem.(Tokyo.), 1996- v. 120, p. 580 586
- Katoh, T., Morita, F: Binding of myosin subfragment 1 to actin. J.Biochem. (Tokyo.), 1996- v. 120, p. 189−192
- Kobayashi, N., Endo, S., Kobayashi, H., Faulstich, H., Wieland, T., Munekata, E:
- Comparative study on the conformation of phalloidin, viroisin, and related derivatives in aqueous solution. Eur.J.Biochem., 1995- v. 232, p. 726−736
- Kraft, T., Xu, S., Brenner, B., Yu, L. C: The effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional x-ray diffraction study on single muscle fibers. Biophys.J., 1999- v. 76, p. 14 941 513
- Kreuz, A. J., Simcox, A., Maughan, D: Alterations in flight muscle ultrastructure and function in Drosophila tropomyosin mutants. J.CellBiol., 1996- v. 135, p. 673−687
- Maciver, S. K: How ADF/cofilin depolymerizes actin filaments. Curr.Opin.Cell
- Biol., 1998- v. 10, p. 140−144
- Mak, A. S., Smillie, L. B., Stewart, G. R: A comparison of the amino acid sequences of rabbit skeletal muscle alpha- and beta-tropomyosins. J.Biol. Chem., 1980- v. 255, p. 3647−3655
- Marston, S. B., Redwood, C. S: The essential role of tropomyosin in cooperative regulation of smooth muscle thin filament activity by caldesmon. J.Biol.Chem., 1993- v. 268, p. 12 317−12 320
- Marston, S. B., Fraser, I. D., Huber, P. A: Smooth muscle caldesmon controls the strong binding interaction between actin-tropomyosin and myosin. J.Biol.Chem., 1994- v. 269, p. 32 104−32 109
- Maruta, S., Henry, G. D., Sykes, B. D., Ikebe, M: Formation of the stable myosin-ADP-aluminum fluoride and myosin-ADP- beryllium fluoride complexes and their analysis using 19 °F NMR. J.Biol.Chem., 1993- v. 268, p. 70 937 100
- Maytum, R., Lehrer, S. S., Geeves, M. A: Cooperativity and switching within the three-state model of muscle regulation. Biochemistry, 1999- v. 38, p. 1102−1110
- McGough, A: F-actin-binding proteins. Curr.Opin.Strnet.Biol., 1998- v. 8, p. 166 176
- McKillop, D. F., Geeves, M. A: Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys.J., 1993- v. 65, p. 693−701
- Mendelson, R., Morris, E.P.: The structure of the acto-myosin subfragment 1complex: results of searches using data from electron microscopy and x-ray crystallography. Proc.Natl.Acad.Sci.U.S.A., 1997- v. 94, p. 8533−8538
- Milligan, R. A., Flicker, P. F: Structural relationships of actin, myosin, andtropomyosin revealed by cryo-electron microscopy. J. Cell Biol., 1987- v. 105, p. 29−39
- Milligan, R. A: Protein-protein interactions in the rigor actomyosin complex. Proc.Natl.Acad.Sci. U.S.A., 1996- v. 93, p. 21−26
- Mo, J. M., Holtzer, M. E., Holtzer, A: Kinetics of self-assembly of alpha alpha-tropomyosin coiled coils from unfolded chains. Proc.Natl.Acad.Sci. U.S.A., 1991- v. 88, p. 916−920
- Monteiro, P. B., Lataro, R. C., Ferro, J. A., Reinach, Fd: Functional alphatropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J.Biol.Chem., 1994- v. 269, p. 10 461−10 466
- Moore, P. B., Huxley, H. E., DeRosier, D. J.: Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J.Mol.Biol, 1970- v. 50, p. 279−295
- Mornet, D., Pantel, P., Audemard, E., Kassab, R: The limited tryptic cleavage of chymotryptic S-l: an approach to the characterization of the actin site in myosin heads. Biochem.Biophys.Res.Commun. 1979- v. 89, p. 925−932
- Murphy, C. T., Spudich, J. A: The sequence of the myosin 50−20K loop affects
- Myosin’s affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry, 1999- v. 38, p. 3785−3792
- Nikolaeva, O. P., Orlov, V. N., Dedova, I. V., Drachev, V. A., Levitsky, D. I.1.teraction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry. Biochem. Mol. Biol. Internat., 1996, v. 40, p. 653 661.
- Novy, R. E., Liu, L. F., Lin, C. S., Helfman, D. M., Lin, J. J: Expression of smooth muscle and nonmuscle tropomyosins in Escherichia coli and characterization of bacterially produced tropomyosins. Biochim.Biophys.Acta, 1993, v. 1162, p. 255−265
- O’Brien, R., Sturtevant, J. M., Wrabl, J., Holtzer, M. E., Holtzer, A: A scanningcalorimetric study of unfolding equilibria in homodimeric chicken gizzard tropomyosins. Biophys.J., 1996, v. 70, p. 2403−2407
- Orlova, A., Egelman, E. H: Structural basis for the destabilization of F-actin byphosphate release following ATP hydrolysis. J.Mol.Biol., 1992, v. 227, p. 1043−1053
- Ostap, E. M., Barnett, V. A., Thomas, D. D: Resolution of three structural states ofspin-labeled myosin in contracting muscle. Biophys.J., 1995, v. 69, p. 177−188
- Otto, J. J: Actin-bundling proteins. Curr.Opin.CellBiol, 1994, v. 6, p. 105−109
- Panusz, H. Т., Graczyk, G., Wilmanska, D., Skarzynski, J: Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities. Anal.Biochem., 1970, v. 35, p. 494−504
- Park, S., Ajtai, K., Burghardt, Т. P: Inhibition of myosin ATPase by metal fluoride complexes. Biochim.Biophys.Acta, 1999, v. 1430, p. 127−140
- Parry, D. A: Letter: Double helix of tropomyosin. Nature, 1975, v. 256, p. 346−347
- Phan, В., Reisler, E: Inhibition of myosin ATPase by beryllium fluoride. Biochemistry, 1992, v. 31, p. 4787−4793
- Phan, В. C., Faller, L. D., Reisler, E: Kinetic and equilibrium analysis of theinteractions of actomyosin subfragment-l.ADP with beryllium fluoride. Biochemistry, 1993, v. 32, p. 7712−7719
- Phan, В. C., Cheung, P., Stafford, W. F., Reisler, E: Complexes of myosinsubfragment-1 with adenosine diphosphate and phosphate analogs: probes of active site and protein conformation. Biophys.Chem., 1996, v. 59, p. 341−349
- Pollard, T. D: Polymerization of ADP-actin. J.CellBiol., 1984, v. 99, p. 769−777
- Pollard, T. D., Weeds, A. G: The rate constant for ATP hydrolysis by polymerized actin. FEBSLett., 1984, v. 170, p. 94−98
- Ponomarev, M. A., Timofeev, V. P., Levitsky, D. I: The difference between ADP-beryllium fluoride and ADP-aluminium fluoride complexes of the spinlabeled myosin sub fragment 1. FEBS Lett., 1995, v. 371, p. 261−263
- Potekhin, S. A., Privalov, P. L: Co-operative blocks in tropomyosin. J.Mol.Biol., 1982, v. 159, p. 519−535
- Privalov, P. L., Tsalkova, T. N: Micro- and macro-stabilities of globular proteins. Nature, 1979, v. 280, p. 693−696
- Privalov, P. L: Stability of proteins. Proteins which do not present a singlecooperative system. Adv. Protein Chem., 1982, v. 35, p. 1−104
- Privalov, P. L., Tiktopulo, E. I., Venyaminov, S. Y., Griko, Y., Makhatadze, G. I., Khechinashvili, N. N: Heat capacity and conformation of proteins in the denatured state. J.Mol.Biol., 1989, v. 205, p. 737−750
- Puius, Y. A., Mahoney, N. M., Almo, S. C: The modular structure of actin-regulatory proteins. Curr.Opin.CellBiol., 1998, v. 10, p. 23−34
- Rayment, I., Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., Holden, H. M: Three-dimensional structure of myosin subfragment-1: a molecular motor. Science, 1993, v. 261, p. 50−58
- Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., Milligan, R. A: Structure of the actin-myosin complex and its implications for muscle contraction. Science, 1993, v. 261, p. 58−65
- Rayment, I: The structural basis of the myosin ATPase activity. J.Biol.Chem., 1996, v. 271, p. 15 850−15 853
- Rebello, C. A., Ludescher, R. D: Influence of tightly bound Mg2+ and Ca2+, nucleotides, and phalloidin on the microsecond torsional flexibility of F-actin. Biochemistry, 1998, v. 37, p. 14 529−14 538
- Rozycki, M. D., Myslik, J. C., Schutt, C. E., Lindberg, U: Structural aspects of actin-binding proteins. Curr.Opin.Cell Biol., 1994, v. 6, p. 87−95
- Ruiz-Opazo, N., Nadal-Ginard, B: Alpha-tropomyosin gene organization. Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms. J.Biol.Chem., 1987, v. 262, p. 47 554 765
- Sanders, C., Burtnick, L. D., Smillie, L. B: Native chicken gizzard tropomyosin ispredominantly a beta gamma- heterodimer. J.Biol. Chem., 1986, v. 261, p. 12 774−12 778
- Schaertl, S., Lehrer, S. S., Geeves, M. A: Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation. Biochemistry, 1995, v. 34, p. 15 890−15 894
- Seymour, J., O’Brien, E. J: Structure of myosin decorated actin filaments and natural thin filaments. J. Muscle Res. Cell Motil., 1985, v. 6, p. 725−755
- Smillie, L. B., Pato, M. D., Pearlstone, J. R., Mak, A. S: Periodicity of alpha-helical potential in tropomyosin sequence correlates with alternating actin binding sites. J.Mol.Biol., 1980, v. 136, p. 199−202
- Smith, C. A., Rayment, I: X-ray structure of the magnesium (II).ADP.vanadatecomplex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry, 1996, v. 35, p. 5404−5417
- Smith, C. W., Marston, S. B: Disassembly and reconstitution of the Ca 2±sensitive thin filaments of vascular smooth muscle. FEBS Lett., 1985, v. 184, p. 115−119
- Spudich, J. A., Watt, S: The regulation of rabbit skeletal muscle contraction. I.
- Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. Biol.Chem., 1971, v. 246, p. 4866−4871
- Squire, J. M., Morris, E. P: A new look at thin filament regulation in vertebrate skeletal muscle. FASEBJ., 1998, v. 12, p. 761−771
- Steinmetz, M. O., Goldie, K. N., Aebi, U: A correlative analysis of actin filamentassembly, structure, and dynamics. J. Cell Biol., 1997, v. 138, p. 559−574
- Sturtevant, J. M., Holtzer, M. E., Holtzer, A: A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin. Biopolymers, 1991, v. 31, p. 489−495
- Sun, H. Q., Kwiatkowska, K., Yin, H. L: Actin monomer binding proteins. Curr. Opin. Cell Biol., 1995, v. 7, p. 102−110
- Takahashi, K., Sturtevant, J. M: Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex. Biochemistry, 1981, v. 20, p. 6185−6190
- Tirion, M. M., ben-Avraham, D: Normal mode analysis of G-actin. J.Mol.Biol., 1993, v. 230, p. 186−195
- Urbancikova, M., Hitchcock-DeGregori, S. E: Requirement of amino-terminal modification for striated muscle alpha- tropomyosin function. J.Biol.Chem., 1994, v. 269, p. 24 310−24 315
- Uyeda, T. Q., Abramson, P. D., Spudich, J. A: The neck region of the myosin motor domain acts as a lever arm to generate movement.
- Proc.Natl.Acad.Sci. U.S.A., 1996, v. 93, p. 4459−4464
- Van Dijk, J., Furch, M., Derancourt, J., Batra, R., Knetsch, M. L., Manstein, D. J.,
- Chaussepied, P: Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II. Eur.J.Biochem., 1999, v. 260, p. 672−683
- Vibert, P., Craig, R., Lehman, W: Steric-model for activation of muscle thin filaments. J.Mol.Biol., 1997, v. 266, p. 8−14
- Weeds, A. G., Taylor, R. S: Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature, 1975, v. 257, p. 54−56
- Wegner, A: Equilibrium of the actin-tropomyosin interaction. J.Mol.Biol., 1979, v. 131, p. 839−853
- Werber, M. M., Peyser, Y. M., Muhlrad, A: Characterization of stable berylliumfluoride, aluminum fluoride, and vanadate containing myosin subfragment 1-nucleotide complexes. Biochemistry, 1992, v. 31, p. 7190−7197
- White, H. D., Belknap, B., Webb, M. R: Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry, 1997, v. 36, p. 11 828−11 836
- Williams, D. L. J., Swenson, C. A: Tropomyosin stability: assignment of thermally induced conformational transitions to separate regions of the molecule. Biochemistry, 1981, v. 20, p. 3856−3864
- Wong, W. W., Doyle, T. C., Reisler, E: Nonspecific weak actomyosin interactions: relocation of charged residues in subdomain 1 of actin does not alter actomyosin function. Biochemistry, 1999, v. 38, p. 1365−1370
- Wriggers, W., Schulten, K: Stability and dynamics of G-actin: back-door waterdiffusion and behavior of a subdomain ¾ loop. Biophys.J., 1997, v. 73, p. 624−639
- Wriggers, W., Schulten, K: Investigating a back door mechanism of actin phosphate release by steered molecular dynamics. Proteins, 1999, v. 35, p. 262−273
- Yanagida, T., Harada, Y., Ishijima, A: Nano-manipulation of actomyosin molecular motors in vitro: a new working principle. Trends.Biochem.Sci., 1993, v. 18, p. 319−324