Insights into translational termination from the structure of RF2 bound to the ribosome

Science

Volumn 322, Issue 5903, 2008, Pages 953-956

  Weixlbaumer, Albert ^a   Jin, Hong ^a   Neubauer, Cajetan ^a   Voorhees, Rebecca M ^a   Petry, Sabine ^a,b   Kelley, Ann C ^a   Ramakrishnan, Venki ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REGULATOR PROTEIN; RELEASE FACTOR 2; RIBOSOME PROTEIN; RIBOSOME PROTEIN 70S; UNCLASSIFIED DRUG;

CATALYSIS; CRYSTAL STRUCTURE; HYDROLYSIS; PEPTIDE; PROTEIN; RNA;

ARTICLE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN SYNTHESIS REGULATION; RIBOSOME; STOP CODON; STRUCTURE ANALYSIS; TRANSLATION REGULATION;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; BIOCATALYSIS; CODON, TERMINATOR; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; PEPTIDE CHAIN TERMINATION, TRANSLATIONAL; PEPTIDE TERMINATION FACTORS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOME SUBUNITS; RIBOSOMES; RNA, BACTERIAL; RNA, TRANSFER; THERMUS THERMOPHILUS;

EID: 55849143658     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1164840     Document Type: Article

References (34)

1. M. R. Capecchi, Proc. Natl. Acad. Sci. U.S.A. 58, 1144 (1967).
2. E. M. Youngman, M. E. McDonald, R. Green, Annu. Rev. Microbiol. 62, 353 (2008).
3. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
4. L. Y. Frolova et al., RNA 5, 1014 (1999).
5. K. Ito, M. Uno, Y. Nakamura, Nature 403, 680 (2000).
6. K. S. Wilson, K. Ito, H. F. Noller, Y. Nakamura, Nat. Struct. Biol. 7, 866 (2000).
7. H. Song et al., Cell 100, 311 (2000).
8. B. Vestergaard et al., Mol. Cell 8, 1375 (2001).
9. U. B. Rawat et al., Nature 421, 87 (2003).
10. B. P. Klaholz et al., Nature 421, 90 (2003).
11. S. Petry et al., Cell 123, 1255 (2005).
12. M. Selmer et al., Science 313, 1935 (2006).
13. Materials and methods are available as supporting material on Science Online.
14. M. Laurberg et al., Nature 454, 852 (2008).
15. G. Zoldak et al., Nucleic Acids Res. 35, 1343 (2007).
16. J. M. Ogle et al., Science 292, 897 (2001).
17. J. M. Ogle, F. V. Murphy, M. J. Tarry, V. Ramakrishnan, Cell 111, 721 (2002).
18. E. M. Youngman, S. L. He, L. J. Nikstad, R. Green, Mol. Cell 28, 533 (2007).
19. D. V. Freistroffer, M. Kwiatkowski, R. H. Buckingham, M. Ehrenberg, Proc. Natl. Acad. Sci. U.S.A. 97, 2046 (2000).
20. K. Ito, M. Uno, Y. Nakamura, Proc. Natl. Acad. Sci. U.S.A. 95, 8165 (1998).
21. J. M. Ogle, V. Ramakrishnan, Annu. Rev. Biochem. 74, 129 (2005).
22. A. V. Zavialov, L. Mora, R. H. Buckingham, M. Ehrenberg, Mol. Cell 10, 789 (2002).
23. J. J. Shaw, R. Green, Mol. Cell 28, 458 (2007).
24. T. M. Schmeing, K. S. Huang, S. A. Strobel, T. A. Steitz, Nature 438, 520 (2005).
25. L. Mora et al., Mol. Microbiol. 47, 267 (2003).
26. S. Trobro, J. Aqvist, Mol. Cell 27, 758 (2007).
27. V. Dincbas-Renqvist et al., EMBO J. 19, 6900 (2000).
28. E. M. Youngman, J. L. Brunelle, A. B. Kochaniak, R. Green, Cell 117, 589 (2004).
29. J. L. Brunelle, J. J. Shaw, E. M. Youngman, R. Green, RNA 14, 1526 (2008).
30. M. Amort et al., Nucleic Acids Res. 35, 5130 (2007).
31. B. Vestergaard et al., Mol. Cell 20, 929 (2005).
32. M. Ejby, M. A. Sorensen, S. Pedersen, Proc. Natl. Acad. Sci. U.S.A. 104, 19410 (2007).
33. I. K. Ali, L. Lancaster, J. Feinberg, S. Joseph, H. F. Noller, Mol. Cell 23, 865 (2006).
34. We thank M. Schmeing for his useful comments and M. Fuchs and C. Schulze-Briese for their help and advice with data collection at the Swiss Light Source. This work was supported by MRC UK, a program grant from the Wellcome Trust, and awards from the Agouron Institute and Louis-Jeantet Foundation. C.N. is supported by a Boehringer-Ingelheim fellowship and R.M.V. is supported by a Gates-Cambridge fellowship. Coordinates for the structure have been deposited in the Protein Data Bank with accession codes 2jl5 to 2jl8. V.R. holds stock options in Rib-X Pharmaceuticals, a company that develops antibacterial drugs that target the ribosome.