Рибосомный белок S26 человека: взаимодействие с собственной пре-м РНК и участие в регуляции ее сплайсинга
Диссертация
Суммарную РНК из плаценты человека выделяли по методу, описанному в работе. Выделение полиаденилированной РНК из суммарной клеточной РНК и синтез первой цепи кДНК с помощью праймера d (T)i2-i8 проводили в соответствие со. стандартными протоколами, описанными в. кДНК rpS26 получали с помощью полимеразной цепной реакции (ПЦР) с использованием набора фирмы «Advanced Biotechnology». В качестве… Читать ещё >
Содержание
- ПРИНЯТЫЕ СОКРАЩЕНИЯ
- ГЛАВА 1. Рибосомные белки эукариот: регуляция экспрессии их генов и внерибосомные функции (Обзор литературы)
- 1. 1. Регуляция экспрессии генов рибосомных белков
- 1. 1. 1. Регуляция на уровне транскрипции
- 1. 1. 2. Регуляция на стадии сплайсинга
- 1. 1. 2. 1. Традиционный сплайсинг
- 1. 1. 2. 2. Альтернативный сплайсинг
- 1. 1. 3. Регуляция на стадии трансляции
- 1. 1. 3. 1. Особенности регуляции трансляции мРНК рибосомных белков
- 1. 1. 3. 2. Структурные элементы мРНК рибосомных белков, участвующие в регуляции трансляции
- 1. 1. 3. 3. Белковые факторы, связывающиеся с 5'-UTR мРНК рибосомных белков
- 1. 1. 3. 4. Роль компонентов аппарата трансляции в регуляции трансляции мРНК рибосомных белков
- 1. 1. Регуляция экспрессии генов рибосомных белков
- 1. 2. Внерибосомные функции рибосомных белков
- 1. 2. 1. Ферментативная активность рибосомных белков
- 1. 2. 2. Связь между рибосомными белками и апоптозом
- 1. 2. 3. Роль рибосомных белков при злокачественной трансформации клеток
- 1. 2. 3. 1. Экспрессия генов рибосомных белков в опухолевых клетках
- 1. 2. 3. 2. Функции рибосомных белков при злокачественной трансформации
- 1. 2. 4. Рибосомные белки как антигены при аутоиммунных заболеваниях
- 1. 2. 5. Участие рибосомных белков в клеточном ответе на вирусную инфекцию
- 1. 2. 6. Влияние рибосомных белков на эмбриональное развитие
- 1. 2. 7. Несистематизированные внерибосомные функции
Список литературы
- Nomura М. Regulation of ribosome biosynthesis in Escherichia coli and Saccharomyces cerevisiae: diversity and common principles // J. Bacteriol. 1999. V.181 P. 6857−6864.
- Yoshihama M., Uechi Т., Asakawa S., Kawasaki K, Kato S., Higa S., Maeda N., Minoshima S., Tanaka Т., Shimizu N. Kenmochi N. The human ribosomal protein genes: sequencing and comparative analysis of 73 genes // Genome Res. 2003. V. 12. P. 379−390.
- Zhao Y., SohnJ.H., Warner J.R. Autoregulation in the biosynthesis of ribosomes // Mol. Cell. Biol. 2003. V. 23. P. 699−707.
- Vilardell J., Chartrand P., Singer R.H., Warner J.R. The odyssey of a regulated transcript // RNA. 2000. V. 6. P. 1773−1780.
- Meyuhas O., Avni D., Shama S. Translational control of ribosomal protein mRNAs in eukaryotes // Translational control / Eds J.W.B. Hershey, M.B. Mathews, N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1996. P. 363−388.
- Bortoluzzi S., d’Alessi F., Romualdi C., Danieli G.A. Differential expression of genes coding for ribosomal proteins in different human tissues // Bioinformatics. 2001. V. 17. P. 1152−1157.
- Грайфер Д.М., Карпова Г. Г., Кнорре ЦТ. Расположение матрицы на рибосоме человека по данным аффинной модификации реакционноспособными аналогами мРНК // Биохимия. 2001. Т.66. Вып. 6. С. 725−744.
- D.C. A map of 75 human ribosomal protein genes // Genome Res. 1998. V. 8. P. 509−523.
- Warner J.R. The economics of ribosome biosynthesis in yeast // Trends Biochem. Sci. 1999. V. 24. P. 437−440.
- Lascaris R.F., Mager W.H., Planta R.J. DNA-binding requirements of the yeast protein Raplp as selected in silico from ribosomal protein gene promoter sequences // Bioinformatics.1999. V. 15. P. 267−277.
- Yarragudi A., Miyake Т., Li R" Morse R.H. Comparison of Abfl and Rapl in chromatin opening and transactivator potentiation in the budding yeast Saccharomyces cerevisiae И Mol. Cell. Biol. 2004. V. 24. P. 9152−9164.
- Li В., Nierras C.R., Warner J.R. Transcriptional elements involved in the repression of ribosomal protein synthesis // Mol. Cell. Biol. 1999. V. 19. P. 5393−5404.
- Lascaris R.F., de Groot E., Hoen P.-В., Mager W.H., Planta R.J. Different roles for Abflp and T-rich promoter element in nucleosome organization of the yeast RPS28A gene // Nucleic Acids Res. 2000. V. 28. P. 1390−1396.
- Shore D. RAP1: a protein regulator in yeast//Trends Genet. 1994. V. 10. P. 408−412.
- Schmelzle Т., Веек Т., Martin D.E., Hall M.N. Activation of the RAS/Cyclic AMP pathway suppresses a TOR deficiency in yeast // Mol. Cell. Biol. 2004. V. 24. P. 338−351.
- Klein C., Struhl K. Protein kinase A mediates growth-regulated expression of yeast ribosomal protein genes by modulating RAP1 transcriptional activity // Mol. Cell. Biol. 1994. V. 14. P. 1920−1928.
- Neuman-Silberberg F.S., Bhattacharya S., Broach J.R. Nutrient availability and the
- RAS/cyclic AMP pathway both induce expression of ribosomal protein genes in Saccharomyces but different mechanisms // Mol. Cell. Biol. 1995. V. 15. P. 3187−3196.
- Mencia M., Moqtaderi Z, Geisberg J. V., Kuras L., Struhl K. Activator-specific recruitment of TFIID and regulation of ribosomal protein genes in yeast // Mol. Cell. 2002. V. 9. P. 823−833.
- Mizuta K., Warner J.R. Continued functioning of the secretory pathway is essential for * ribosome synthesis // Mol. Cell. Biol. 1994. V. 14. P. 2493−2502.
- Mizuta К., Tsujii R., Warner J.R., Nishiyama M. The C-terminal silencing domain of Raplp is essential for the repression of ribosomal protein genes in response to a defect in secretory pathway//Nucleic Acids Res. 1998. V. 26. P. 1063−1069.
- Fingerman I., Nagaraj V., Norrisa D" Vershon A.K. Sfpl plays a key role in yeast ribosome biogenesis // Eukar. Cell. 2003. V. 2. P. 1061−1068.
- Jorgensen P., Nishikawa J.L., Breitkreutz B.J., Tyers M. Systematic identification of pathways that couple cell growth and division in yeast // Science. 2002. V. 297. P. 395−400.
- Marion R.M., Regev A., Segal E., Barash Y., Koller D., Friedman N., O’Shea K. Sfpl is a stress- and nutrient-sensitive regulator of ribosomal protein gene expression // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 14 315−14 322.
- Jorgensen P., Rupes I., Sharom J.г., Shcneper L., Broach J.R., Tyers M. A dynamic transcriptional network communicates growth potentional to ribosome synthesis and critical cell size // Genes Dev. 2004. V. 18. P. 2491−2505.
- Schawalder S.B., Kabani M., Howald I., Choudhury U, Werner M., Shore D. Growthregulated recruitment of the essential yeast ribosomal protein gene activator Ifhl // Nature. 2004. V. 432. P. 1058−1061.
- Wade J.T., Hall D.B., Struhl K. The transcription factor Ifhl is a key regulator of yeast ribosomal protein genes //Nature. 2004. V. 432. P. 1054−1058.
- Rudra D., Zhao Y., Warner J.R. Central role of Ifhlp-Fhllp interaction in the synthesis of • yeast ribosomal proteins // EMBO J. 2005. V. 24. P. 533−542.
- Durocher D., Jackson S.P. The FHA domain // FEBS Lett. 2002. V. 513. P. 58−66.
- ReidJ.L., Iyer V.R., Brown P.O., Struhl K. Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esal histoneacetylase // Mol Cell. 2000. V. 6. P. 1297−1307.
- Sienna N. Larson D.E., Sells B.H. Dexamethasone stimulates ribosomal protein L32 gene transcription in rat myoblasts//Mol. Cell. Endocrinol. 2000. V. 167. P. 127−137.
- Curcic D., Glibetic M., Larson D.E., Sells B.H. GA-binding protein is involved in altered expression of ribosomal protein L32 gene // J. Cell. Biol. 1997. V. 65. P. 287−307.
- Tasheva E.S., Roufa D.J. Regulation of human RPS14 transcription by intronic antisense RNAs and ribosomal protein S14 // Genes Dev. 1995. V. 9. P. 304−316.
- Jurica M.S., Moore M.J. Pre-mRNA splicing: awash in sea of proteins // Mol. Cell. 2003. V. 12. P. 5−14.
- Caffarelli E., Fragapane P., Gehring C., Bozzoni I. The accumulation of mature RNA for the Xenopus laevis ribosomal protein LI is controlled at the level of splicing and turnover of the precursor RNA. // EMBO J. 1987. V. 6. P. 3493−3498.
- Presutti C., Ciafre S.-A., Bozzoni I. The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA // EMBO J. 1991. V. 10. P. 2215−2221.
- Presutti C., Villa Т., Hall D" Petrica C., Bozzoni I. Identification of the m-elements mediating the autogenous control of ribosomal protein L2 mRNA stability in yeast // EMBO J. 1995. V. 14. P. 4022−4030.
- Dabeva M.D., Warner J.R. Ribosomal protein L32 of Saccharomyces cerevisiae regulates both splicing and translation of its own transcript. // J. Biol. Chem. 1993. V. 268. P. 1 966 919 674.
- Li H., Dalai S., KohlerJ., Vilardell J., White S.A. Characterization of the pre-mRNA binding site for yeast ribosomal protein L32: the importance of a purine-rich internal loop. // J. Mol. Biol. 1995. V. 250. P. 447−459.
- Vilardell J., Warner J.R. Ribosomal protein L32 of Saccaromyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA // Mol. Cell. Biol. 1997. V. 17. P. 1959−1965.
- Mao H., Williamson J.R. Local folding coupled to RNA binding in the yeast ribosomal protein L30 // J. Mol. Biol. 1999. V. 292. P. 345−359.
- Mao H., White S.A., Williamson J.R. A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex // Nat. Struct. Biol. 1999. V. 6. P. 11 391 147.
- Li Z, Paulovich A. G, Woolford J.L.Jr. Feedback inhibition of the yeast ribosomal protein gene CRY2 is mediated by the nucleotide sequence and secondary structure of CRY2 pre-mRNA // Mol. Cell. Biol. 1995. V. 15. P. 6454−6464.
- Zheng Z.-M. Regulation of alternative RNA splicing by exon definition and exon sequences in viral and mammalian gene expression // J. Biomed. Sci. 2003. V. 11. P. 278−294.
- Hilleren P., Parker R. Mechanisms of mRNA surveillance in eukaryotes. Annu. Rev. Genet. 1999. V. 33. P. 229−260.
- Lee C., Atanelov L., Modrek В., Xing Y. ASAP: the alternative splicing annotation project // Nucl. Acids Res. 2003. V. 31. P. 101−105.
- Lewis В.P., Green R.E., Brenner S.E. Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans // Proc. Natl. Acad. Sci. USA. 2003. V. 100. P. 189−192.
- Aw W.-B., Roufa D.J. The gene encoding human ribosomal protein S24 and tissue-specific expression of differentially spliced mRNAs // Gene. 1996. V. 169. P. 257−262.
- Mitrovich Q.M., Anderson P. Unproductively spliced ribosomal protein mRNAs are natural targets of mRNA surveillance in C. elegans II Genes Dev. 2000. V. 14. P. 2173−2184.
- Angelastro J.M., Klimaschewski L., TangS., Vitolo OV" Weisman ТА., DonlinLT., Shelanski
- ML., Green L.A. Identification of diverse nerve growth factor-regulated genes by serial analysis of gene expression (SAGE) profiling // Proc. Natl. Acad. Sci. USA. 2000. V. 97. P. 1 042 410 429.
- Levi-Montalcini R. The saga of the nerve growth factor // Neuroreport. 1998. V. 9. P. R71−83.
- Al-Atia G.R., Fruscoloni P., Jacobs-Lorena M. Translational regulation of mRNAs forribosomal proteins during early Drosophila development // Biochemistry. 1985. V. 24. P. 57 985 803.
- Loreni F., Amaldi F. Translational regulation of ribosomal protein synthesis in Xenopus cultured cells: mRNA relocation between polysomes and RNP during nutritional shifts // Eur. J. Biochem. 1992. V. 205. P. 1027−1032.
- Loreni F., Francesconi A., Amaldi F. Coordinate translational regulation in the synthesis of elongation factor la and ribosomal protein in Xenopus laevis И Nucl. Acids Res. 1993. V. 21. P. 4721−4725.
- Amara F.M., Sun J., Wright J. A. Defining a novel c/s-element in the 3'-untranslated region of mammalian ribonucleotide reductase component R2 mRNA // J. Biol. Chem. 1996. V. 271. P.20 126−20 131.
- Levi S., Avni D., Hariharan N., Perry R.P., Meyuhas O. Oligipyrimidine tract at the 5' end of mammalian ribosomal protein mRNAs is required for their translational control // Proc. Natl. Acad. Sci. 1991. V. 88. P. 3319−3323.
- Kaspar R.L., Kakegava Т., Cranston H., Morris D.R., White M.W. A regulatory cis element and a specific binding factor involved in the mitogenic control of murine ribosomal protein L32 translation // J. Biol. Chem. 1992. V. 267. P. 508−514.
- Severson W.E., Mascolo P.L., White M. W. Lymphocyte p56L32 is a RNA/DNA binding protein which interacts with conserved elements of the murine L32 ribosomal protein mRNA.// Eur. J. Biochem. 1995. V. 229. P. 426−432.
- Patton J.G., Mayer S.A., Tempst P., and Nadal-Ginard B. Characterization and molecular • cloning of polypyrimidine tract binding protein: a component of a complex necessary for premRNA splicing//Genes Dev. 1991. V. 5. P. 1237−1251.
- Pellizzoni L., Lotti F., Maras В., Pierandrei-Amaldi P. Cellular nucleic acid binding protein binds a conserved region of the 5' UTR of Xenopus laevis ribosomal protein mRNAs // J. Mol. Biol. 1997. V. 267. P. 264−275.t
- Pellizzoni L., Lotti F., Rutjes S.A., Pierandrei-Amaldi P. Involvement of the Xenopus laevis Ro60 autoantigen in the alternative interaction of La and CNBP proteins with the 5' UTR of L4 ribosomal protein mRNA //J Mol. Biol. 1998. V. 281. P. 593−608.
- Pruijn G.J.M., Slobbe R.L., van Venrooij W.J. Analysis of protein-RNA interaction within Ro ribonucleoprotein complexes//Nucleic Acids Res. 1991. V. 19. P. 5173−5180.
- Cardinali В., Carissimi C., Gravina P., Pierandrei-Amaldi P. La protein is associated with terminal oligopyrimidine mRNAs in actively translating polysomes // J. Biol. Chem. 2003. V. 278. P. 35 145−35 151.
- Crossio С., BoylP.P., Loreni F., Pierandrei-Amaldi P., Amaldi F. La protein has a positive effect on the translation of TOP mRNA in vivo H Nucl. Acids Res. 2000. V. 28. P. 2927−2934.
- Duncan R., Milburn S.C., Hershey J.W.B. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4 °F suggest a role in translational control. Heat shock effects on eIF-4 °F // J. Biol. Chem. 1987. V. 262. P. 380−388.
- Shama S., Avni D., Frederickson R.M., Sonenberg N. Meyuhas O. Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells // Gene Expr. 1995. V. 4. P. 241−252.
- Reboud A.M., Dubost S., Reboud J.P. Identification of the proteins interacting with tRNA in rat liver small ribosomal subunits // FEBS Lett. 1983. V. 158. P. 285−288.
- Westermann P., Heumann W., Bommer W.A., Bielka H" Nygard O., Hultin T. Cross-linking of initiation factor eIF-2 to proteins of the small subunit of rat liver ribosomes // FEBS lett. 1979. V 97. P. 101−104.
- Nygars O., Nilsson L., Westermann P. Characterisation of the ribosomal binding site for eukaryotic elongation factor 2 by chemical cross-linking // Biochim. Biophys. Acta. 1987. V. 910. P. 245−53.
- Stewart M.J., Thomas G. Mitogenesis and protein synthesis: A role for ribosomal protein S6 phosphorylation? // BioEssays. 1994. V. 16. P. 1−7.
- Terada N. Patel H.R., Takase K, Kohno K, Nairin A.C., and Gelfand E.W. Rapamicin selectively inhibits translation of mRNA encoding elongation factors and ribosomal proteins // Proc. Natl. Acad. Sci. 1994. V.91.P. 11 477−11 481.
- Je/feries H.B., Reinhard C., Kozma S.C., and Thomas G. Paramycin selectively represses ^ translation of the «polypyrimidine tract» mRNA family // Proc. Natl. Acad. Sci. 1994. V. 91. P.4441−4445.
- Jefferies H.B.J., Fumagalli S., Dennis P.В., Reinhard C., PearsonR.B., and Thomas G. Rapamicin suppresses 5'TOP mRNA translation through inhibition p70s6k // EMBO J. 1997. V. 16. P. 3693−3704.
- Reiter A.K., Anthony T.G., Anthony J.C., Jefferson L.S., Kimball S.R. The mTOR signaling # pathway mediates control of ribosomal protein mRNA translation in rat liver // Int. J. Biochem.
- Cell Biol. 2004. V. 36. P. 2169−2179.
- Hyman L.E., Wormington W.M. Translational inactivation of ribosomal protein mRNAs during Xenopus oocyte maturation // Genes Dev. 1988. V. 2. P. 598−605.
- Minden S.L., Bassuk E.L., Nadler S.P. Lithium intoxication: a coordinated treatment approach // J. Gen. Intern. Med. 1993. V. 8. P. 33−40.
- Stolovich M" Lerer Т., Bolkier K, Cohen H" Meyuhas O. Lithium can relieve translational repression of TOP mRNAs, elicited by various blocks along the cell cycle, in GSK3- and S6K-independent manner // J. Biol. Chem. 2005. V. 280. P. 5336−5342.
- Caldarola S., Amaldi F., Proud C.G., Loreni F. Translation regulation of terminaloligopyrimidine mRNAs induced by serum ad amino acids involves distinct signaling event // J. Biol. Chem. 2004. V. 279. P. 13 522−13 531.
- Kakegaxva Т., Ito M., Hayakawa A., Matsuda M., Tamura S., Saito H., Kaspar R.L., Kobayashi H. Rapamycin induces binding activity to the terminal oligopyrimidine tract of ribosomal protein mRNA in rats // Arch. Biochem. Biophys. 2002. V. 402. P. 77−83.
- Kim J., Chubatsu L.S., Admon A., Stahl J., Fellows R., Linn S. Implication of mammalian ^ ribosomal protein S3 in the processing of DNA damage // J. Biol. Chem. 1995. V. 270. P. 1 362 013 629.
- Wilson D.M.lll, Deutsch W.A., Ketley M.R. Drosophila ribosomal protein S3 contains an activity that cleaves DNA at apurinic/apyrimidinic sites // J. Biol. Chem. 1994. V. 269. P. 2 535 925 364.
- Jung S.O., Lee J.Y., Kim J. Yeast ribosomal protein S3 has an endonuclease activity on • AP DNA//Mol. Cells. 2001. V. 12. P. 84−90.
- Yacoub A., Kelley M.R., Deutsch W.A. Drosophila ribosomal protein P0 containsьapurinic/apyrimidinic endonuclease activity // Nucl. Acids Res. 1996. V. 24. P. 4295−4303.
- Grabowski D.T., Pieper R.O., Futscher B. W., Deutsch W.A., Erickson L.C., Kelley M.R. Expression of ribosomal phosphoprotein P0 is induced by antitumor agents and increased in Mer- human tumor cell lines // Carcinogenesis. 1992. V. 13. P. 259−263.
- Nadano D., Sato T.-A. Caspase-3-dependent and -independent degradation of 28S ribosomal RNA may be involved in the inhibition of protein synthesis during apoptosis initiated by death receptor engagement // J. Biol. Chem. 2000. V. 275. P. 13 967−13 973.
- Nishida J., Shiratsuchi A., Nadano D., Sato T.-A., Nakanishi Y. Structural change of ribosomes during apoptosis: degradation and externalization of ribosomal proteins in doxorubicin-treated Jurkat cells // J.Biochem. 2002. V. 131. P. 485−493.
- Spahn C.M.T., Beckmann R., Eswar N. Penczek P.A., Sali A., Blobel G., Frank J. Structure of the 80S ribosome from Saccharomyces cerevisiae tRNA-ribosome and subunitsubunit interaction // Cell. 2001. V. 107. P. 373−386.
- Malygin A.A., Shaulo D.D., Karpova G.G. Proteins S7, S10, S16 and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt. // Biochim.Biophys.Acta. 2000. V.1494. P. 213−216.
- Yamamoto T. Molecular mechanism of monocyte predominant infiltration in chronic inflammation: mediation by a novel monocyte chemotactic factor, S19 ribosomal protein dimer // Parhol. Int. 2000. V. 50. P. 863−871.
- Shibuya Y., Shiokawa M., Nishiura H" Nishimura Т., Nishino N" Okabe H., Takagi K" Yamamoto T. Identification of receptor-binding sites of monocyte chemotactic S19 ribosomal protein dimer//Am. J. Pathol. 2001. V. 159. P. 2293−2301.
- Khanna N" Reddy V.G., Tuteja N. Singh N. Differantial gene expression in apoptosis: identification of ribosomal protein S29 as an apoptotic inducer // Biochem. Biophys. Res. Commun. 2000. V. 277. P. 476−486.
- Zhou ZD., Bao L., Liu D.G., Li M.Q., Ge Y. Z, Huang Y.L., Liu W.Y. Low content of protein S29 in ribosomes of human lung cancer cell line A549: detected by two-dimensional electrophoresis //Protein Pept. Lett. 2003. V. 10. P. 91−97.
- Schimmer A.D., Hedley L.Z., Penn M.D., Minden M.D. Receptor- and mitochondrial-mediated apoptosis in acute leukemia: a translational view// Blood. 2001. V. 98. P. 3541−3553.
- KangJ.J., Schaber M.D., Srinivasula S.M., Alnemri E.S., Litwack G., Hall D.J., Bjornsti M.A. Cascades of mammalian caspase activation in the yeast Saccharomyces cerevisiae II J. Biol. Chem. 1999. V. 274. P. 3189−3198.
- Khanna N., Sen S., Sharma H., Singh N. S29 ribosomal protein induces apoptosis in H520 cells and sensitizes them to chemotherapy // Biochem. Biophys. Res. Commun. 2003. V. 304. P. 26−35.
- Naora H., Naora H. Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity? // Immunol. Cell Biol. 1999. V. 77. P. 197−205.
- Song D., Sakamoto S., Taniguci T. Inhibition of Poly (ADP-ribose) polymerase activity by Bcl-2 in association with ribosomal protein S3a // Biochemistry. 2002. V. 41. P. 929−934.
- Ни Z, Minden M.D., McCulloch E.A., Stahl J. Regulation of drug sensitivity by ribosomal protein S3a//Blood. 2000. V. 95. P. 1047−1055.
- Kuo M.L., Shen S.C., Yang C.H., Chuang S.E., Cheng A.L., Huang T.S. Bcl-2 prevents topoisomerase II inhibitor GL331-induced apoptosis is mediated by down-regulation of poly (ADP-ribose)polymerase activity//Oncogene. 1998. V. 17. P. 2225−2234.
- Jang C.-Y., Lee J. Y., Kim J. RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis // FEBS Lett. 2004. V. 560. P. 81−85.
- Neumann F., Krawinkel U. Constitutive expression of human ribosomal protein L7 arrests the cell cycle in G1 and induces apoptosis in Jurkat T-lymphoma cells // Exp. Cell. Res.1997. V. 230. P. 252−61
- Berghoefer-Hochheimer Y., Zurek C., Woelfl S., Hemmerich P., Munder T. L7 protein is a coregulator of vitamin D receptor-retionoid X receptor-mediated transactivation // J. Cell. Biol. 1998. V. 69. P. 1−12.ri
- Lopez C.D., Martinovsky G., Naumovski L. Inhibition of cell death by ribosomal protein L35a // Cancer Res. 2002. V. 180. P. 195−202.
- Gross A., McDonnell J.M., Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis//Genes Dev. 1999. V. 13. P. 1899−1991.
- Zhang L., Zhou W., Velculescu V.E., Kern S.E., Hruban R.H., Hamilton S.R., Vogelstein
- В., Kinzler K. W. Gene expression profiles in normal and cancer cells // Science. 1997. V. 276. P. 1268−1272.
- Amsterdam A., Sadler K.C., Lai K., Farrington S., Bronson R.T., Lees J.A., Hopkins N. Many ribosomal protein genes are cancer genes in zebrafish // PLoS Biol. 2004. V. 2. P. 6 900 698.
- Barnard G.F., Staniunas R.J., Mori M., Puder M., Jessup M.J., Steele G.D.Jr., Chen L.B. Gastric and hepatocellular carcinomas do not overexpress the same ribosomal protein messenger RNAs as colonic carcinoma // Cancer Res. 1993. V. 53. P. 4048−4052.
- Barnard G.F., Staniunas R.J., Bao S., Mafune K., Steele G.D.J.r, Gollan J.L., Chen L.B. Increased expression of human ribosomal phosphoprotein P0 messenger RNA in hepatocellular carcinoma and colon carcinoma // Cancer Res. 1992. V. 52. P. 3067−3072.
- Starkey C.R., Levy L.S. Identification of differentially expressed genes in T-lymphoid malignancies in an animal model system // Int. J. Cancer. 1995. V. 62. P. 325−331.
- Lian Z., Liu J., Li I, Li X, Tufan N.L.S., Wu M.-C., Wang H.-Y., Arbuthot P., Kew M., Feitelson M.A. Human SI 5a expression is upregulated by hepatitis В virus X protein I I Mol. Carcinogen. 2004. V. 40. P. 34−46.
- Diamantis I.D., McGandy C.E., Chen T.J., Liaw Y.F., Gudat F., Bianchi L. Hepatitis В X-gene expression in hepatocellular carcinoma // J. Hepatol. 1992. V. 15 P. 400−403.
- Pellegrini R., Martignone S., Merand S., Colnaghi M.I. Laminin receptor expression and function in small-cell lung carcinoma // Int. J. Cancer. 1994. V. 8. P. 116−120.
- Castronovo V. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis//Invasion Metastas. 1993. V. 13. P. 1−30.
- Moll U.M., Petrenko O. The MDM-2-p53 interaction // Mol. Cancer Res. 2003. V. 1. P. 1001−1008.
- Loging W.T., Reisman D. Elevated expression of ribosomal protein genes L37, RPP-1, and S2 in the presence of mutant p53 // Cancer Epidem. Biomark. Prevent. 1999. V8. P. 10 111 016.
- Modugno M" Tagliabue E., Ardini E" Вето V., Galmozzi E., De Bortoli M" Castronovo V., Menard S. p53-dependent downregulation of metastasis-associated laminin receptor // Oncogene. 2002. V. 21. P. 7478−7487.
- Shi Y" Zhai H., Wang X, Wu H., Ning X., Han Y., Zhang D., Xiao В., Wu K, Fan D. Multidrug-resistance-associated protein MGrl-Ag is identical to the human 37-kDa laminin receptor precursor // Cell. Mol. Life Sci. 2002. V. 59. P. 1577−1583.
- Iwakuma Т., Lozano G. MDM2, an introduction // Mol. Cancer Res. 2003 V. 1. P. 9 931 000.
- Dai M.-S., Lu H. Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5 // J. Biol. Chem. 2004. V. 279. P. 44 475−44 482.
- Zhang Y., Wolf G.W., Bhat K, Jin A., Allio Т., Burkhart W.A., Xiong Y. Ribosomal protein LI 1 negatively regulates oncoprotein MDM2 and mediates a 53-dependent ribosomal-stress checkpoint pathway // Mol. Cell. Biol. 2003. V. 23. P. 8902−8912.
- Dai M.-S., Zeng S.X., Jin Y, SunX-X, David L., Lu H. Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition // Mol. Cell Biol. 2004. V. 24. P. 7654−7668.
- Jin A., Itahana K, O’Keefe K, Zhang Y. Inhibition of HDM2 and activation of p53 by ribosomal protein L23 // Mol. Cell. Biol. 2004. V. 24. P. 7669−7680.
- Bhat K.P., Itahana K, Jin A., Zhang Y. Essential role of ribosomal protein Lll in mediating growth inhibition-induced p53 activation // EMBO J. 2004. V. 23. P. 2402−2412.
- Voit R., Kuhn A., Sander E.E., Grummt I. Activation of mammalian ribosomal gene transcription requires phosphorylation of the nucleolar transcription factor UBF // Nucleic. Acids Res. 1995. V. 23. P. 2593−2599.
- Ahn B.H., Kim Т.Н., Bae Y.S. Mapping of the interaction domain of the protein kinase CKII p subunit with target proteins // Mol. Cells. 2001. V. 12. P. 158−63.
- Soulet F., Saati T.A., Roga S., Amalric F., Bouche G. Fibroblast growth factor-2 interacts with free ribosomal protein S19 // Biochem. Biophys. Res. Commun. 2001. V. 289. P. 591−596.
- Williams B.R. Signal transduction via PKR // Science’s STKE. 2001. V. 89. P. 1−10.
- Meurs E.F., Galabru J., Barber G.N., Katze M.G., Hovanessian A.G. Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase // Proc. Natl. Acad. Sci. USA 1993. V. 90. P. 232−236.
- Proud C.G. PKR: a new name and new roles // Trends Biochem. Sci. 1995. V. 20. P. 241 246.
- Koromilas A.E., Roy S., Barber G.N., Katze M.G., Sonenberg N. Malignat transformation by a mutant of the interferon-inducible double-stranded RNA dependent protein kinase // Science. 1992. V. 257. 1685−1689.
- Kumar K.U., Srivastava S.P., Kaufman R.J. Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein LI 8 // Mol. Cell. Biol. 1999. V.19. P. 1116−1125.
- Hamaguchi I., Ooka A., Brun J., Richter J., Dahl N., Karlsson S. Gene transfer improves erythroid development in ribosomal protein S19-deficient Diamond-Blackfan anemia // Blood. 2002. V. 100. P. 2724−2731.
- Koga M., Shichijo S., Yamada A., Ashihara J., Sawamizu H., Kusukawa J., Itoh K. Identification of ribosomal proteins S2 and LlOa as tumor antigens recognized by HLA-A26-restricted CTL // Tissue Antigens. 2003. V. 61. P. 136−145.
- Marks P.A., Richon V.M., Rifkind R.A. Cell cycle regulatory proteins are targets for induced differentiation of transformed cells: Molecular and clinical studies employing hybrid polar compounds // Int. J. Hematol. 1996. V. 63. PI-17.
- The L.C., Bedwell A.E., Iseberg D.A., Gordon C., Emery P., Charles P.J., Harper M" Amos N., Williams B.D. Antibodies to protein P in systemic lupus erythematosus // Ann. Rheum. Dis. 1992. V. 51. P. 489−494.
- Derksen R.H., van Dam A.P., Gmelig Myling F.H., Bijlsma J.W., Smeenk R.J. A prospective study on antiribosomal P proteins in two cases of familial lupus and recurrent psychosis // Ann. Rheum. Dis. 1990. V. 49. P. 779−782.
- Elkon K.B., Parnassa A.P., Foster C. Lupus autoantibodies target ribosomal P proteins // J. Exp. Med. 1985. V. 162. P. 459−471.
- Isshi K., Hirohata S. Differential roles of the anti-ribosomal P antibody and anti-neuronal antibody in the pathogenesis of central nervous system involvement in systemic lupus erythematosu // Artthritis. Rheum. 1998. V. 41. P. 1819−1827.
- Martin A., Reichlin M. Fluctuations of antibody to ribosomal 'P' proteins correlate with appearance and remission of nephritis in SLE // Lupus. 1996. V. 5. P. 22−29.
- Koren E., Reichlin M.W., Koscec M., Fugate R.D., Reichlin M Autoantibodies to the ribosomal P proteins react with a plasma membrane related target on human cells // J. Clin. Invest. 1992. V. 89. P. 1236−1241.
- Koscec M., Koren E., Wolfson-Reichlen M., Fugate R.D., Trieu E., Targoffl.N., Reichlin M. Autoantibodies to ribosomal P proteins penetrate into live hepatocytes and cause cellular dysfunction in culture//J. Immunol. 1997. V. 159. P. 2033−2041.
- Chan E., Ко О., Lawton J., Lau C. The use of anti-ribosomal P antibodies in the diagnosis of cerebral lupus superiority of western blotting over enzyme-linked immunosorbent assay // Hong Kong Med J. 1998. V. 4. P. 145−150.
- Reichlin M. Ribosomal P antibodies and CNS lupus // Lupus. 2003. V. 12. P. 916−918.
- Hasegawa Я, Uchiumi Т., Sato Т., Saito A., Nakano M., Gejyo F. Autoantibody against ribosomal protein L14 in patients with systemic lupus erythematosus // Clin. Exp. Rheumat. 2002. V. 20. P. 139−144.
- IVitte S., Krawinkel U. Specific interaction of the autoantigen L7 with multi-zink finger protein ZNF7 and ribosomal protein S7 // J. Biol. Chem. 1997. V. 272. P. 22 243−22 247.
- Anderson C.J., Neas B.R., Uchiumi Т., Stafford A. Autoantibodies to the 20-kDa ribosomal proteins: identification, characterization, and new aspects on prevalence in systemic lupus erythematosus//Clin. Immun. 2001. V. 98. P. 249−257.
- Apcher S., Fahraeus R., Manoury B. Epstein-Barr virus: exploiting the immune system by interfering with defective ribosomal products 11 Microb. Infect. 2004. V. 6. P. 1212−1218.
- Clarke P.A., Schwemmle M., Schickinger J., Hilse K, Clemens M.J. Binding of Epstein-Barr virus small RNA EBER-1 to the double-stranded RNA-activated protein kinase DAI // Nucleic Acids Res. 1991. V. 19. P. 243−248.
- Nanbo A., Inoue K, Adachi-Takasawa K., Takada К Epstein-Barr virus RNA confers resistence to interferon-A-induced apoptosis in Burkitt’s lymphoma // EMBO J. 2002. V. 21. P. 954−965.
- Toczyski D.P., Matera A.G., Ward D.C., Steitz J.A. The Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBF-infected human В lymphocytes // Proc. Natl. Acad. Sci. USA. 1994. V.91. P. 3463−3467.
- Elia A., Vyas J., Laing K.G., Clemens M.J. Ribosomal protein L22 inhibits regulation of cellular activities by the Epstein-Barr virus small RNA EBER-1 // Eur. J. Biochem. 2004. V. 271. P. 1895−1905.
- Rao C.N., Barsky S.H., Terranova V.P., Liotta L.A. Isolation of a tumor cell laminin receptor//Biochem. Biophys. Res. Common. 1983. V. 111. P. 804−808.
- Rao C.N., Castronovo V., Schmitt M.C., Wewer U.M., Claysmith A.P., Liotta L.A., Sobel M.E. Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor // 1989. Biochemistry. V 28. P. 7476−7486.
- Tohgo A., Takasawa S., Munakata H., Yonekura H., Hayashi N., Okamoto H. Structural determination and characterization of a 40 kDa protein isolated from rat 40S ribosomal subunit // FEBS Lett. 1994. V. 340. P. 133−138.
- Kinoshita K, Kaneda Y" Sato M., Saeki Y., Wataya-Kaneda M., Hoffmann A, LBP-p40 binds DNA tightly through associations with histones H2A, H2B, and H4 // Biochem. Biophys. Res. Commun. 1998. V. 253. P. 277−282.
- Gloe Т., Riedmayr S., Sohn H.-Y., Pohl U. The 67-kDa laminin-binding protein is involved in shear stress-dependent endothelial nitric-oxide synthase expression // J. Biol. Chem. 1999. V. 274. P. 15 996−16 002.
- Бондаренко Е.И., Протопопова Е. В., Некрасов В. М., Локтев В. Б. Моноклональные антитела к рекомбинантному ламининсвязывающему белку человека. Получение и иммунохимическая характеристика // Вестник РАМН. 2004. Т. 8. С. 31−35.
- Bridges C.B., Morgan Т.Н. The third chromosome group of mutant characters of Drosophila melanogaster II Carnegie Inst. Wash. Publ. 1923.
- Marygold S.J., Coelho C.M., Leevers S.J. Genetic Analysis of RpL38 and RpL5, Two Minute Genes Located in the Centric Heterochromatin of Chromosome 2 of Drosophila melanogaster II Genetics. 2005. V. 169. P. 683−695.
- Enerly E., Larsson J., Lambertsson A. Silencing the Drosophila ribosomal protein L14 gene using targeted RNA interference causes distinct somatic anomalies // Gene. 2003. V. 320. P. 41−48.
- Saeboe-Larssen S., Lyamouri M., Merriam J., Oksvold M.P., Lambertsson A. Ribosomal protein insufficiency and the minute syndrome in Drosophila: a dose-response relationship // Genetics. 1998. V. 148. P. 1215−1224.
- Oliver E.R., Saunders T.L., Tarle S.A., Glaser T. Ribosomal protein L24 defect in Belly spot and tail (BST), a mouse Minute 11 Development. 2004. V. 131. P. 3907−3920.
- Matsson H., Davey E.J., Draptchinskaia N. Hamagichi I., OokaA., Leveen P., Forsberg E., Karlsson S., Dahl N. Target disruption of the ribosomal protein S19 gene is lethal prior to implantation // Mol. Cell. Biol. 2004. V. 24. P. 4032−4037.
- Mazumder В., Mukhopadhyay C.K., Prok A., Cathcart M.K., Fox P.L. Induction of ceruloplasmin synthesis by IFN-y in human monocytic cells// J. Immunol. 1997. V. 159. P. 19 381 944.
- Klebanoff S.J. Bactericidal effect of Fe2+, ceruloplasmin, and phosphate 11 Arch. Biochem. Biophys. 1992. V. 295. P. 302−308.
- Mazumder В., Fox P.L. Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells 11 Mol. Cell. Biol. 1999. V. 19. P. 6898−6905.
- Mazumder В., Sampath P., Seshadri V., maitra R.K., DiColreto P.E., Fox P.L. Regulated release of LI3a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control // Cell. 2003. V. 115. P. 187−198.
- Kusui K., Sasaki H" Adachi R., Matsui S., Yamamoto K., Yamaguchi Т., Kasahara Т., Suzuki K. Ribosomal protein SI8 identified as a cofilin-binding protein by using phage display library//Mol. Cell. Biochem. 2004. V. 262. P. 187−193.
- Bamburg J.R. Proteins of the ADF/cofilin family: essential regulators of actin dynamics // Annu. Rev. Cell. Dev. Biol. 1999. V. 15. P. 185−230.
- Pei L. Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and novel human homologue of DnaJ in testicular cells // J. Biol. Chem. 1999. V. 274. P. 31 513 158.
- Pei L" Melmed S. Isolation and characterization of a pituitary tumor-transforming gene (PTTG) // Mol. Endocrinol. 1997. V. 11. P. 433−441.
- Weinberg R.A. The retinoblastoma protein and cell cycle control // Cell. 1995. V. 81. P. 323−330.
- Moorthamer M., Chaudhuri B. Identification of ribosomal protein L34 as a novel Cdk5 inhibitor// Biochem. Biophys. Res. Commun. 1999. V. 255. P. 631−638.
- Koyama Y., Katagiri S., hanai S., Uchida K., Miwa M. Poly (ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and L23a, with unique histone-like amino-terminal extension // Gene. 1999. V. 226. P. 339−345.
- Miwa M., Hanai S., Poltronieri P., Uchida M., Uchida K. Functional analysis of poly (ADP-ribose) polymerase in Drosophila melanogaster II Mol. Cell. Biochem. 1999. V. 193. P. 103−107.
- Myokai F., Oyama M" Nishimura F., Ohira Т., Yamamoto Т., Arai Т., Takashiba S. Murayama Y. Unique genes induced by mechanical stress in periodontal ligament cells // J. Periodont. Res. 2003. V. 38. P. 255−261.
- Brosche M" Strid A. The mRNA-binding ribosomal protein S26 as a molecular marker in plants: molecular cloning, sequencing and differential gene expression during environmental stress // Biochim. Biophys. Acta. 1999. V. 1445. P. 342−344.
- Zhu Y, Lin H., Li Z., Wang M., Lao J. Modulation of expression of ribosomal protein L7a (L7a) ethanol in human breast cancer cells // Breast Cancer Res. Treat. 2001. V. 69. P. 29−38.
- Lang C.H., Pruznak A.M., Deshpande N. Palopoli M.M., Frost R.A., Vary T.C. Alcohol intoxication impairs phosphorylation of S6K1 and S6 in skeletal muscle independently of ethanol metabolism //Alcohol. Clin. Exp. Res. 2004. V. 28. P. 1758−1767.
- Ju Z., Dunham R.A., Liu Z. Differential gene expression in the brain of channel catfish (Ictalurus punctatus) in response to cold acclimation // Mol. Genet. Genomics. 2002. V. 268. P. 87−95.
- Madjar J.-J., Arpin M., Buisson M., Reboud J.-P. Spot position of rat liver ribosomal proteins by four different two-dimentional electrophoresis in polyacrylamide gel // Mol. Gen. Genet. 1979. V.171. P.121−134.
- Chen G.T., Inouye M. Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli // Genes Dev. 1994. V. 8. P. 2641−2652.
- O’Mullane L., Eperon J.C. The pre-mRNA 5' cap determines whether U6 small nuclear RNA succeeds U1 small nuclear ribonucleoprotein particle at 5' splice sites // Mol. Cell. Biol. 1998. V. 18. P. 7510−7520.
- Zuker M. Mfold web server for nucleic acid folding and hybridization prediction // Nucleic Acids Res. 2003. V. 31. P. 3406−3415.
- Филипенко M.JI., Виниченко H.A., Карпова Г. Г., Мертвецов Н. П., Амалди Ф. Клонирование и структурно-функциональный анализ гена рибосомного белка S26 человека//Генетика. 1998. Т. 34. С. 469−474.
- Liu Z.-R., Sargueil В., Smith С. W.J. Methylene blue-mediated cross-linking of proteins to double-stranded RNA // Methods Enzymol. 2000. V. 318. P. 35−47.
- Бабкина Г. Т., Владимиров C.H., Грайфер Д. М., Матасова Н. Б., Смоленская И. А., Карпова Г. Г. Выделение рибосом и субчастиц из плаценты человека и определение их функциональной активности // Изв. Сиб. Отд. АН СССР. 1989. Вып. 2. С. 92−98.
- Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 //Nature. 1970. V. 277. P. 680−685.
- Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction//Anal. Biochem. 1987. — V. 162. — P. 156−159.
- Sambrook J., Russell D. Molecular cloning: a laboratory manual // Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 2001.
- Кислых В. К, Рамазанов Ю. А., Майстренко В. Ф., Мертвецов Н. П. Вихревой биореактор «БИОК». I. Опыт культивирования штамма E. coli BL21 (DE3) pZZSA, продуцирующего рекомбинантный ангиогенин человека // Биотехнология. 2001. № 3. С. 72−79.1. БЛАГОДАРНОСТИ
- В качестве своей признательности автор выражает Малыгину Алексею Аркадьевичу свое искреннее восхищение его бескрайней научной эрудицией, творческим воодушевлением и способностью критически осмысливать полученные результаты.
- Особое удовольствие автору приносит возможность поблагодарить Яныпину Дарью Дмитриевну за доброе отношение и помощь в оформление диссертации.
- Автор искренне благодарит всех и каждого, кто работал и продолжает работать в самой замечательной Лаборатории структуры и функции рибосом и от чистого сердца желает им успехов во всех их делах.