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Взаимодействия белков с РНК – структурный компьютерный анализ

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рис.2.2.3. Структура комплекса S15-16SрРНК (S15 T3C мутант)

 

 

 

 

 

 

 

 

 

 

 

Выводы:

 

  1. Получен и обработан набор дифракционных данных для комплекса S15-16SрРНК (S15 T3C мутант).
  2. Методом молекулярного замещения определена структура комплекса.
  3. Показано, что рибосомный белок комплекса S15 связывается с 16S рРНК в двух пространственно удалённых участках.
  4. Показано, что мутация Т3С не изменяет пространственной структуры комплекса и структуры РНК-белкового интерфейса.

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Список литературы:

 

  1. Серганов А.А. (1997) Изучение РНК-связывающих свойств рибосомного белка S15 из Thermus thermophilus. Диссертация, МГУ.
  2. Anston A.A., Otridge J., Brzozowski A.M., Dodson E.J., Dodson G.G., Wilson K.S., Smith T.M., Yang M., Kurecki T., Gollnick P. (1995). Biochemestry. 18: 693-700
  3. Argos P. & Rossmann M.G. (1980) in “Theory and Practice of Direct Methods in Crystallography” (Ladd and Palmer, eds.), pp.361-417. Plenum, New York.
  4. Bentley G.A. & Houndusse A. (1992), Acta Cryst. A48, 312-322.
  5. Blundell T.L. & Johnson L.N. (1974) Protein Crystallography. Academic Press, New York.
  6. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., Warren G.L. (1998) Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination. Acta Cryst. D54, 909-921.
  7. Brunger A.T., Milburn M.V., Tong L., de Vos A.M., Jancarik J., Yamazumi Z., Nishimura S., Ohtsuka E., Kim S.-H. (1990), Proc. Natl. Acad. Sci. USA 87, 4849-4853.
  8. Burd C.G. Dreifuss G. (1994). Conserved structures and diversity of functions of RNA-binding proteins. Science 265: 615-620
  9. Bycroft M., Grunert S., Murzin A., Proctor M., Johnston D. (1995). NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14: 3563-3571
  10. Bycroft M., Hubbard T.J.P., Proctor M., Freund S.M.V., Murzin A. (1997). The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell 88: 235-242
  11. Castellano E., Oliva G., Navaza J. (1992), J. Appl. Cryst. 25, 281.
  12. Cate J.H., Gooding A.R., Podell E., Zhou K., Golden B.L., Szewczak A.A., Kundrot C.E., CechT.R., Doudna J.A. (1996). RNA tertiary structure mediation by adenosine platforms. Science 273: 1696-1699
  13. Chang G. & Lewis M. (1994), Acta Cryst. D50, 667-674.
  14. Chang G. & Lewis M. (1997) Molecular Replacement Using Genetic Algorithms. Acta Cryst. D53, 279-289.
  15. Crowther R.A. & Blow D.M. (1967), Acta Cryst. 23, 544-548.
  16. Crowther R.A. (1972) in “The Molecular Replacement Method”, Int. Sci. Rev. No.13 (Rossmann M.G., ed.). Gordon & Breach, New York.
  17. Draper D.E. (1995). Protein-RNA recognition. Annu. Rev. Biochem. 64: 593-620
  18. Draper D.E. (1996) Ribosomal protein-RNA interactions. In Ribosomal RNA: structure, evolution, processing and function in protein biosynthesis. Eds. Zimmermann R.A., Dahlberg A.E. Boca Raton, Florida, CRC Press, 171-198
  19. Franklin C., Shi J.P., Shimmel P. (1992). Overlapping nucleotide determinante for specific aminocylation of RNA. Science. 225: 1121-1125
  20. Fujinaga M. & Read R.J. (1987), J. Appl. Cryst. 20, 517-521.
  21. Harada Y., Lifchitz A., Berthou J., Jolles P. (1981), Acta Cryst. A37, 398-406.
  22. Huber R. (1965), Acta Cryst. A19, 353-356.
  23. Kjems J., Egebjerg J., Christiansen J. (1998) Laboratory techniques in biochemistry and molecular biology. Elsevier, 237
  24. Kim J.L., Nikolov D.B., Burley S.K. (1993). Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365: 520-527
  25. Kirkpatrick S., Gelatt C.D. Jr & Vecchi M.P. (1983), Science, 220, 671-680.
  26. Kissinger C.R., Gehlhaar D.K., Fogel D.B. (1999) Rapid automated molecular replacement by evolutionary search. Acta Cryst. D55, 484-491.
  27. Marino J.P., Gregorian R.S., Csankovski G., Grothers D.M. (1995). Ent helix formation between RNA hairpins with complementary loops. Science 268: 1448-1254
  28. Metropolis N., Rosenbluth A.W., Rosenbluth M.N., Teller A. & Teller E. (1953), J. Chem. Phys. 21, 1087-1092.
  29. Miller S.T., Hogle J.M. & Filman D.J. (1996), Acta Cryst. D52, 235-251.
  30. Musco G., stier G., Joseph C., Morelli M.A.C., Nilges M., Gibson T.J., Pastore A.. (1996) Thre-dimensional structure and stability of the KH domain: molecular insight into the fragile X syndrome. Cell 85: 237-245
  31. Nevskaya, N., Tishchenko, S., Nikulin, A., Al-Karadaghi, S., Liljas, A., Ehresmann, B., Ehresmann, C., Garber, M., Nikonov, S. (1998) Crystal Structure of Ribosomal Protein S8 from Thermus Thermophilus Reveals a High Degree of Structural Conservation of a Specific RNA Binding Site. J.Mol.Biol. 279, 233-244.
  32. Normanly J., Abelson J. (1989). TRNA identity. Annu. Rev. Biochem. 58: 1029-1049
  33. Powell M.J.D. (1977), Math. Programming, 12, 241-254.
  34. Read R.J. (1997) Model Phases: Probabilities and Bias. In Methods in Enzymology, 277, 110-128, Academic Press.
  35. Read R.J. & Schierbeek A.J. (1988), J. Appl. Cryst. 21, 490-495.
  36. Rossmann M.G., Blow D.M., Harding M.M., Coller E. (1964), Acta Cryst. 17, 338-342.
  37. Rossmann M.G. & Blow D.M. (1962), Acta Cryst. 15, 24-31
  38. Schindelin H., Marahiel M.A., Heinemann U. (1993). Universal nucleic acid-binding domain revealed by crystal structure og the B.subtilis major cold-shock domain. Nature 364: 164-168
  39. Seeman N., Rosenberg J.M., Rich A. (1976). Sequence-specific recgnition of double helical nucleic acids by proteins. Pros. Natl, Acad. USA 73: 804-808
  40. von Hippel P.H., McGhee J.D. (1972). DNA-protein interactions. Annu. Rev. Biochem. 41: 231-298
  41. Weeks K.M., Crothers D.M. (1993). Major grove accessibility of RNA. Science 261: 1574-1577