Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 17, 1999, Pages 9586-9590

  Rodnina, Marina V ^a   Savelsbergh, Andreas ^a   Matassova, Natalia B ^a,c   Katunin, Vladimir I ^b   Semenkov, Yuri P ^b   Wintermeyer, Wolfgang ^a  

^a UNIVERSITY OF WITTEN HERDECKE   (Germany)

^b PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^c INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; THIOSTREPTON; TRANSFER RNA;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RIBOSOME; RNA TRANSLATION;

ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GTP PHOSPHOHYDROLASE-LINKED ELONGATION FACTORS; GUANOSINE TRIPHOSPHATE; KINETICS; PEPTIDE ELONGATION FACTOR G; PEPTIDE ELONGATION FACTORS; PHOSPHATES; RIBOSOMES; RNA, RIBOSOMAL, 23S; RNA, TRANSFER, AMINO ACYL; THIOSTREPTON; TRANSLOCATION, GENETIC;

EID: 0033578321     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.17.9586     Document Type: Article

References (42)

1. Moazed, D., Robertson, J. M. & Noller, H. F. (1988) Nature (London) 334, 362-364.
2. Sköld, S. E. (1983) Nucleic Acids Res. 11, 4923-4932.
3. Egebjerg, J., Douthwaite, S. R., Liljas, A. & Garrett, R. A. (1990) J. Mol. Biol. 213, 275-288.
4. Traut, R. R., Dey, D., Bochkariov, D. E., Oleinikov, A. V., Jokhadze, G. G., Hamman, B. & Jameson, D. (1995) Biochem. Cell Biol. 73, 949-958.
5. Egebjerg, J., Douthwaite, S. & Garrett, R. A. (1989) EMBO J. 8, 607-611.
6. Ryan, P. C., Lu, M. & Draper, D. E. (1991) J. Mol. Biol. 221, 1257-1268.
7. Thompson, J. & Cundliffe, E. (1991) Biochimie 73, 1131-1135.
8. Thompson, J., Musters, W., Cundliffe, E. & Dahlberg, A. E. (1993) EMBO J. 12, 1499-1504.
9. Rosendahl, G. & Douthwaite, S. (1993) J. Mol. Biol. 234, 1013-1020.
10. Xing, Y. & Draper, D. E. (1995) J. Mol. Biol. 249, 319-331.
11. Gale, E. F., Cundliffe, E., Reynolds, P. E., Richmond, M. H. & Waring, M. (1981) The Molecular Basis of Antibiotic Action (Wiley, London), pp. 402-457.
12. Rodnina, M. V. & Wintermeyer, W. (1995) Proc. Natl. Acad. Sci. USA 92, 1945-1949.
13. Borowski, C., Rodnina, M. V. & Wintermeyer, W. (1996) Proc. Natl. Acad. Sci. USA 93, 4202-4206.
14. Soffientini, A., Lorenzetti, R., Gastaldo, L., Parlett, J. H., Spurio, R., La Teana, A. & Islam, K. (1994) Protein Expression Purif. 5, 118-124.
15. Calogero, R. A., Pon, C. L., Canonaco, M. A. & Gualerzi, C. O. (1988) Proc. Natl. Acad. Sci. USA 85, 6427-6431.
16. Rodnina, M. V., Semenkov, Y. P. & Wintermeyer, W. (1994) Anal. Biochem. 219, 380-381.
17. Brune, M., Hunter, J. L., Corrie, J. E. & Webb, M. R. (1994) Biochemistry 33, 8262-8271.
18. Rodnina, M. V., Savelsbergh, A., Katunin, V. I. & Wintermeyer, W. (1997) Nature (London) 385, 37-41.
19. Stern, S., Moazed, D. & Noller, H. F. (1988) Methods Enzymol. 164, 481-489.
20. Pestka, S. (1970) Biochem. Biophys. Res. Commun. 40, 667-674.
21. Naaktgeboren, N., Roobol, K., Gubbens, J. & Voorma, H. O. (1976) Eur. J. Biochem. 70, 39-47.
22. Moazed, D. & Noller, H. F. (1989) Nature (London) 342, 142-148.
23. Wilson, K. S. & Noller, H. F. (1998) Cell 92, 337-349.
24. Baca, O. G., Rohrbach, M. S. & Bodley, J. W. (1976) Biochemistry 15, 4570-4574.
25. Brot, N. (1977) in Molecular Mechanisms of Protein Synthesis, eds. Weissbach, H. & Pestka, S. (Academic, New York), pp. 375-411.
26. Cundliffe, E. (1986) in Structure, Function and Genetics of Ribosomes, eds. Hardesty, B. & Kramer, G. (Springer, New York), pp. 586-604.
27. Bodley, J. W., Lin, L. & Highland, J. H. (1970) Biochem. Biophys. Res. Commun. 41, 1406-1411.
28. Highland, J. H., Lin, L. & Bodley, J. W. (1971) Biochemistry 10, 4404-4409.
29. Cundliffe, E. & Thompson, J. (1981) Eur. J. Biochem. 118, 47-52.
30. Thompson, J. (1995) in Ribosomal RNA. Structure, Evolution, Processing, and Function in Protein Biosynthesis, eds. Zimmermann, R. A. & Dahlberg, A. E. (CRC, Boca Raton, FL), pp. 311-325.
31. Campuzano, S., Vazquez, D. & Modolell, J. (1979) Biochemistry 18, 1570-1574.
32. Lin, L. & Bodley, J. W. (1976) J. Biol. Chem. 251, 1795-1798.
33. Hausner, T. P., Geigenmuller, U. & Nierhaus, K. H. (1988) J. Biol. Chem. 263, 13103-13111.
34. Ryan, P. C. & Draper, D. E. (1989) Biochemistry 28, 9949-9956.
35. Wang, Y. X., Lu, M. & Draper, D. E. (1993) Biochemistry 32, 12279-12282.
36. Wimberly, B. T., Guymon, R., McCutcheon, J. P., White, S. W. & Ramakrishnan, V. (1999) Cell 97, 491-502.
37. Conn, G. L., Draper, D. E., Lattman, E. E. & Gittis, A. G. (1999) Science 284, 1171-1174.
38. Draper, D. E., Xing, Y. & Laing, L. G. (1995) J. Mol. Biol. 249, 231-238.
39. Draper, D. E. & Xing, Y. (1995) Nucleic Acids Symp. Ser. 33, 5-7.
40. Porse, B. T., Leviev, I., Mankin, A. S. & Garrett, R. A. (1998) J. Mol. Biol. 276, 391-404.
41. Miller, S. P. & Bodley, J. W. (1991) Nucleic Acids Res. 19, 1657-1660.
42. Cundliffe, E. (1971) Biochem. Biophys. Res. Commun. 44, 912-917.