A cryo-electron microscopic study of ribosome-bound termination factor RF2

Nature

Volumn 421, Issue 6918, 2003, Pages 87-90

  Rawat, Urmila B S ^a,b   Zavialov, Andrey V ^c   Sengupta, Jayati ^b   Valle, Mikel ^a,b   Grassucci, Robert A ^a,b   Linde, Jamie ^b   Vestergaard, Bente ^d   Ehrenberg, Måns ^c   Frank, Joachim ^a,b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b WADSWORTH CENTER   (United States)

^c UPPSALA UNIVERSITY   (Sweden)

^d AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ELECTRON MICROSCOPY; ENZYMES; SYNTHESIS (CHEMICAL); X RAYS;

GENETIC INFORMATIONS;

RNA;

MESSENGER RNA; PEPTIDYLTRANSFERASE; TRANSCRIPTION FACTOR; TRANSCRIPTION TERMINATION PROTEIN RELEASE FACTOR 2; UNCLASSIFIED DRUG;

PROTEIN;

ACCURACY; AMINO ACID SEQUENCE; ARTICLE; CRYOELECTRON MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN SECRETION; PROTEIN SYNTHESIS; RIBOSOME; RIBOSOME SUBUNIT; RNA TRANSLATION; STOP CODON; TRANSCRIPTION TERMINATION; X RAY ANALYSIS;

EID: 0347721768     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01224     Document Type: Article

References (28)

1. Kisselev, L. L. & Buckingham, R. H. Translational termination comes of age. Trends Biochem. Sci. 25, 561-566 (2000).
2. Zavialov, A. V., Mora, L., Buckingham, R. M. & Ehrenberg, M. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell 10, 789-798 (2002).
3. Ito, K., Ebihara, K. & Nakamura, Y. A tripeptide anticodon deciphers stop codons in messenger RNA. Nature 403, 680-684 (2000).
4. Vestergaard, B. et al. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol. Cell 8, 1375-1382 (2001).
5. Zavialov, A. V., Buckingham, R. H. & Ehrenberg, M. A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107, 115-124 (2001).
6. Wimberly, B. T., Guymon, R., McCutcheon, J. P., White, S. W. & Ramakrishnan, V. R. A detailed view of the ribosomal active site: the structure of the L1 t-RNA complex. Cell 97, 491-502 (1999).
7. Gerstein, M., Lesk, A. M. & Chothia, C. Structural mechanisms for domain movements in proteins. Biochemistry 33, 6739-6749 (1994).
8. Ramakrishnan, V. Ribosome structure and the mechanism of translation. Cell 108, 557-572 (2002).
9. 2 terminal domain of Escherichia coli ribosomal protein L11. J. Biol. Chem. 259, 7317-7324 (1984).
10. Brot, N., Tate, W. P., Caskey, C. T. & Weissbach, H. Requirement for ribosomal proteins L7 and L12 in peptide-chain termination. Proc. Natl Acad. Sci. USA 71, 89-92 (1974).
11. Arkov, A. L. & Murgola, E. J. Ribosomal RNAs in translation termination: facts and hypothesis. Biochemistry (Moscow) 64, 1354-1359 (1999).
12. Seit-Nebi, A., Frolova, L., Justesen, J. & Kisselev, L. Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosomal binding but not for stop codon recognition. Nucleic Acids Res. 29, 3982-3987 (2001).
13. Song, H. et al. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100, 311-321 (2000).
14. Nissen, P., Hansen, J., Ban, N., Moore, P. B. & Steitz, T. A. The structural basis of ribosome activity in peptide bond synthesis. Science 289, 920-930 (2000).
15. Yusupov, M. M. et al. Crystal structure of the ribosome at 5.5 Å resolution. Science 4, 897-902 (2001).
16. Drugeon, G. et al. Eukaryotic release factor 1 (eRF1) abolishes readthrough and competes with suppressor tRNAs at all the three termination codons in messenger RNA. Nucleic Acids Res. 25, 2254-2258 (1997).
17. Tate, W. P., Greuer, B. & Brimacombe, R. Codon recognition in polypeptide chain termination: site directed cross linking of termination codon to Escherichia coli release factor 2. Nucleic Acids Res. 18, 6537-6544 (1990).
18. Wilson, K. S., Ito, K., Noller, H. F. & Nakamura, Y. Functional sites of interaction between release factor RF1 and the ribosome. Nature Struct. Biol. 7, 866-870 (2000).
19. Ito, K., Ebihara, K., Uno, M. & Nakamura, Y. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc Natl Acad. Sci. USA 93, 5443-5448 (1996).
20. Jelenc, P. C. & Kurland, C. G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci. USA 76, 3174-3178 (1979).
21. Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
22. Orlova, E. V. et al. Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. J. Mol. Biol. 271, 417-437 (1997).
23. Gabashvili, I. S. et al. Solution structure of the E coli 70S ribosome at 11.5 Å resolution. Cell 100, 537-549 (2000).
24. Jones, T. A., Zhou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
25. Nissen, P., Hansen, J., Ban, N., Moore, P. B. & Steitz, T. A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289, 905-920 (2000).
26. Wimberly, B. T. et al. Structure of the 30S ribosomal subunit. Nature 407, 327-339 (2000).
27. Yusupova, G. Z., Yusupov, M. M., Cate, J. H. & Noller, H. F. The path of messenger RNA through the ribosome. Cell 106, 233-241 (2001).
28. Carson, M. Ribbons 2.0. J. Appl. Cryst. 24, 103-106 (1991).