How the ribosome hands the A-site tRNA to the P site during EF-G-catalyzed translocation

Science

Volumn 345, Issue 6201, 2014, Pages 1188-1191

  Zhou, Jie ^a   Lancaster, Laura ^a   Donohue, John Paul ^a   Noller, Harry F ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL RNA; FUSIDIC ACID; MESSENGER RNA; NEOMYCIN; RIBOSOME RNA; RNA 16S; RNA 23S; RNA HELICASE; TRANSFER RNA; ELONGATION FACTOR G;

CRYSTAL STRUCTURE; PROTEIN; RNA;

ANTICODON; ARTICLE; BACTERIAL TRANSLOCATION; BASE PAIRING; BINDING SITE; CATALYSIS; CODON; CRYSTAL STRUCTURE; DIFFRACTION; NONHUMAN; PRIORITY JOURNAL; RIBOSOME; RNA STRUCTURE; THERMUS THERMOPHILUS; CHEMISTRY; CONFORMATION; LARGE RIBOSOMAL SUBUNIT; METABOLISM; PROTEIN CONFORMATION; PROTEIN SYNTHESIS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

ANTICODON; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTOR G; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; RIBOSOME SUBUNITS, LARGE, BACTERIAL; RNA, MESSENGER; RNA, TRANSFER; THERMUS THERMOPHILUS;

EID: 84907187230     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1255030     Document Type: Article

References (30)

1. M. V. Rodnina, A. Savelsbergh, V. I. Katunin, W. Wintermeyer, Nature 385, 37-41 (1997).
2. D. Moazed, H. F. Noller, Nature 342, 142-148 (1989).
3. J. Frank, R. K. Agrawal, Nature 406, 318-322 (2000).
4. M. Valle et al., Cell 114, 123-134 (2003).
5. X. Agirrezabala et al., Mol. Cell 32, 190-197 (2008).
6. P. Julián et al., Proc. Natl. Acad. Sci. U.S.A. 105, 16924-16927 (2008).
7. D. N. Ermolenko et al., J. Mol. Biol. 370, 530-540 (2007).
8. B. S. Schuwirth et al., Science 310, 827-834 (2005).
9. A. H. Ratje et al., Nature 468, 713-716 (2010).
10. J. Zhou, L. Lancaster, J. P. Donohue, H. F. Noller, Science 340, 1236086 (2013).
11. D. J. Ramrath et al., Proc. Natl. Acad. Sci. U.S.A. 110, 20964-20969 (2013).
12. Y. Chen, S. Feng, V. Kumar, R. Ero, Y. G. Gao, Nat. Struct. Mol. Biol. 20, 1077-1084 (2013).
13. D. S. Tourigny, I. S. Fernández, A. C. Kelley, V. Ramakrishnan, Science 340, 1235490 (2013).
14. A. Pulk, J. H. Cate, Science 340, 1235970 (2013).
15. Y. G. Gao et al., Science 326, 694-699 (2009).
16. A. F. Brilot, A. A. Korostelev, D. N. Ermolenko, N. Grigorieff, Proc. Natl. Acad. Sci. U.S.A. 110, 20994-20999 (2013).
17. L. B. Jenner, N. Demeshkina, G. Yusupova, M. Yusupov, Nat. Struct. Mol. Biol. 17, 555-560 (2010).
18. M. Selmer et al., Science 313, 1935-1942 (2006).
19. V. Berk, W. Zhang, R. D. Pai, J. H. Cate, Proc. Natl. Acad. Sci. U.S.A. 103, 15830-15834 (2006).
20. B. R. Cunha, F. Peske, W. Holtkamp, W. Wintermeyer, M. V. Rodnina, Translation 1, e24315 (2013).
21. Z. Guo, H. F. Noller, Proc. Natl. Acad. Sci. U.S.A. 109, 20391-20394 (2012).
22. J. M. Ogle et al., Science 292, 897-902 (2001).
23. P. K. Khade, S. Joseph, Nat. Struct. Mol. Biol. 18, 1300-1302 (2011).
24. S. Takyar, R. P. Hickerson, H. F. Noller, Cell 120, 49-58 (2005).
25. R. R. Samaha, R. Green, H. F. Noller, Nature 377, 309-314 (1995).
26. D. F. Kim, R. Green, Mol. Cell 4, 859-864 (1999).
27. J. L. Hansen, T. M. Schmeing, P. B. Moore, T. A. Steitz, Proc. Natl. Acad. Sci. U.S.A. 99, 11670-11675 (2002).
28. D. Pan, S. V. Kirillov, B. S. Cooperman, Mol. Cell 25, 519-529 (2007).
29. W. Holtkamp et al., EMBO J. 33, 1073-1085 (2014).
30. L. V. Bock et al., Nat. Struct. Mol. Biol. 20, 1390-1396 (2013).