A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation

Journal of Biological Chemistry

Volumn 286, Issue 24, 2011, Pages 21697-21705

  Ticu, Cristina ^a   Murataliev, Marat ^a   Nechifor, Roxana ^a   Wilson, Kevin S ^a,b  

^a UNIVERSITY OF ALBERTA   (Canada)

^b OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO ACID RESIDUES; CELLULAR GROWTH; ELONGATION FACTOR; FUSIDIC ACID; GTP HYDROLYSIS; INTER-DOMAIN; TRANSLATION FACTORS;

AMINO ACIDS; ANTIBIOTICS; BACTERIOLOGY; MACROMOLECULES;

HYDROLYSIS;

ALANINE; ELONGATION FACTOR G; FUSIDIC ACID; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MESSENGER RNA; MOCIMYCIN; PHENYLALANINE;

AMINO ACID ANALYSIS; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENETIC CONSERVATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; RESIDUE ANALYSIS; RIBOSWITCH; RNA TRANSLATION; RNA TRANSPORT; STAPHYLOCOCCUS AUREUS; THERMUS THERMOPHILUS;

ANTI-BACTERIAL AGENTS; CATALYTIC DOMAIN; ESCHERICHIA COLI; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MUTATION; PEPTIDE ELONGATION FACTOR G; PHENYLALANINE; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RIBOSOMES; RNA, MESSENGER; TRANSLOCATION, GENETIC;

BACTERIA (MICROORGANISMS);

EID: 79958763710     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.214056     Document Type: Article

References (40)

1. Fischbach, M. A., and Walsh, C. T. (2009) Science 325, 1089-1093
2. Turnidge, J. (1999) Int. J. Antimicrob. Agents 12, S23-S34
3. Johanson, U., and Hughes, D. (1994) Gene 143, 55-59
4. Nagaev, I., Björkman, J., Andersson, D. I., and Hughes, D. (2001) Mol. Microbiol. 40, 433-439
5. Besier, S., Ludwig, A., Brade, V., and Wichelhaus, T. A. (2003) Mol. Microbiol. 47, 463-469
6. Lannergård, J., Norström, T., and Hughes, D. (2009) Antimicrob. Agents Chemother. 53, 2059-2065
7. Castanheira, M., Watters, A. A., Bell, J. M., Turnidge, J. D., and Jones, R. N. (2010) Antimicrob. Agents Chemother. 54, 3614-3617
8. Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A. T., Nagaev, I., Hughes, D., and Liljas, A. (2000) J. Mol. Biol. 303, 593-603
9. Chen, Y., Koripella, R. K., Sanyal, S., and Selmer, M. (2010) FEBS J. 277, 3789-3803
10. Willie, G. R., Richman, N., Godtfredsen, W. P., and Bodley, J. W. (1975) Biochemistry 14, 1713-1718
11. Gao, Y. G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., and Ramakrishnan, V. (2009) Science 326, 694-699
12. Andersson, D. I., and Hughes, D. (2010) Nat. Rev. Microbiol. 8, 260-271
13. Macvanin, M., Johanson, U., Ehrenberg, M., and Hughes, D. (2000) Mol. Microbiol. 37, 98-107
14. Johanson, U., Aevarsson, A., Liljas, A., and Hughes, D. (1996) J. Mol. Biol. 258, 420-432
15. Björkman, J., Nagaev, I., Berg, O. G., Hughes, D., and Andersson, D. I. (2000) Science 287, 1479-1482
16. Martemyanov, K. A., Liljas, A., Yarunin, A. S., and Gudkov, A. T. (2001) J. Biol. Chem. 276, 28774-28778
17. Wilson, K. S., and Nechifor, R. (2004) J. Mol. Biol. 337, 15-30
18. Nechifor, R., Murataliev, M., and Wilson, K. S. (2007) J. Biol. Chem. 282, 36998-37005
19. Nguyen, B., Ticu, C., and Wilson, K. S. (2010) J. Mol. Biol. 397, 1245-1260
20. Jelenc, P. C., and Kurland, C. G. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 3174-3178
21. Wilden, B., Savelsbergh, A., Rodnina, M. V., and Wintermeyer, W. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 13670-13675
22. Moazed, D., Robertson, J. M., and Noller, H. F. (1988) Nature 334, 362-364
23. Vetter, I. R., and Wittinghofer, A. (2001) Science 294, 1299-1304
24. Rodnina, M. V., Savelsbergh, A., Katunin, V. I., and Wintermeyer, W. (1997) Nature 385, 37-41
25. Connell, S. R., Takemoto, C., Wilson, D. N., Wang, H., Murayama, K., Terada, T., Shirouzu, M., Rost, M., Schüler, M., Giesebrecht, J., Dabrowski, M., Mielke, T., Fucini, P., Yokoyama, S., and Spahn, C. M. (2007) Mol. Cell 25, 751-764
26. Ticu, C., Nechifor, R., Nguyen, B., Desrosiers, M., and Wilson, K. S. (2009) EMBO J. 28, 2053-2065
27. Hansson, S., Singh, R., Gudkov, A. T., Liljas, A., and Logan, D. T. (2005) J. Mol. Biol. 348, 939-949
28. Rohrback, M. S., and Bodley, J. W. (1976) Biochemistry 15, 4565-4569
29. Daviter, T., Wieden, H. J., and Rodnina, M. V. (2003) J. Mol. Biol. 332, 689-699
30. Berchtold, H., Reshetnikova, L., Reiser, C. O., Schirmer, N. K., Sprinzl, M., and Hilgenfeld, R. (1993) Nature 365, 126-132
31. Voorhees, R. M., Schmeing, T. M., Kelley, A. C., and Ramakrishnan, V. (2010) Science 330, 835-838
32. Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F., and Nyborg, J. (1995) Science 270, 1464-1472
33. Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y. G., Murphy, F. V., 4th, Weir, J. R., and Ramakrishnan, V. (2009) Science 326, 688-694
34. Martemyanov, K. A., and Gudkov, A. T. (2000) J. Biol. Chem. 275, 35820-35824
35. Mohr, D., Wintermeyer, W., and Rodnina, M. V. (2002) Biochemistry 41, 12520-12528
36. Valle, M., Zavialov, A., Sengupta, J., Rawat, U., Ehrenberg, M., and Frank, J. (2003) Cell 114, 123-134
37. Frank, J., Gao, H., Sengupta, J., Gao, N., and Taylor, D. J. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 19671-19678
38. Wolf, H., Chinali, G., and Parmeggiani, A. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 4910-4914
39. Vogeley, L., Palm, G. J., Mesters, J. R., and Hilgenfeld, R. (2001) J. Biol. Chem. 276, 17149-17155
40. Hansson, S., Singh, R., Gudkov, A. T., Liljas, A., and Logan, D. T. (2005) FEBS Lett. 579, 4492-4497