A cryo-electron microscopic study of ribosome-bound termination factor RF2
10.1038/nature01224
Crossref journal-article
Springer Science and Business Media LLC
Nature (297)
Bibliography

Rawat, U. B. S., Zavialov, A. V., Sengupta, J., Valle, M., Grassucci, R. A., Linde, J., Vestergaard, B., Ehrenberg, M., & Frank, J. (2003). A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature, 421(6918), 87–90.

Authors 9
  1. Urmila B. S. Rawat (first)
  2. Andrey V. Zavialov (additional)
  3. Jayati Sengupta (additional)
  4. Mikel Valle (additional)
  5. Robert A. Grassucci (additional)
  6. Jamie Linde (additional)
  7. Bente Vestergaard (additional)
  8. Måns Ehrenberg (additional)
  9. Joachim Frank (additional)
References 28 Referenced 204
  1. Kisselev, L. L. & Buckingham, R. H. Translational termination comes of age. Trends Biochem. Sci. 25, 561–566 (2000) (10.1016/S0968-0004(00)01669-8) / Trends Biochem. Sci. by LL Kisselev (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) (10.1016/S1097-2765(02)00691-3) / Mol. Cell by AV Zavialov (2002)
  3. Ito, K., Ebihara, K. & Nakamura, Y. A tripeptide anticodon deciphers stop codons in messenger RNA. Nature 403, 680–684 (2000) (10.1038/35001115) / Nature by K Ito (2000)
  4. Vestergaard, B. et al. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol. Cell 8, 1375–1382 (2001) (10.1016/S1097-2765(01)00415-4) / Mol. Cell by B Vestergaard (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) (10.1016/S0092-8674(01)00508-6) / Cell by AV Zavialov (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 L11–RNA complex. Cell 97, 491–502 (1999) (10.1016/S0092-8674(00)80759-X) / Cell by BT Wimberly (1999)
  7. Gerstein, M., Lesk, A. M. & Chothia, C. Structural mechanisms for domain movements in proteins. Biochemistry 33, 6739–6749 (1994) (10.1021/bi00188a001) / Biochemistry by M Gerstein (1994)
  8. Ramakrishnan, V. Ribosome structure and the mechanism of translation. Cell 108, 557–572 (2002) (10.1016/S0092-8674(02)00619-0) / Cell by V Ramakrishnan (2002)
  9. Tate, W. P., Dognin, M. J., Noah, M., Stöffler-Meilicke, M. & Stöffler, G. The NH2 terminal domain of Escherichia coli ribosomal protein L11. J. Biol. Chem. 259, 7317–7324 (1984) (10.1016/S0021-9258(17)39874-5) / J. Biol. Chem. by WP Tate (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) (10.1073/pnas.71.1.89) / Proc. Natl Acad. Sci. USA by N Brot (1974)
  11. Arkov, A. L. & Murgola, E. J. Ribosomal RNAs in translation termination: facts and hypothesis. Biochemistry (Moscow) 64, 1354–1359 (1999) / Biochemistry (Moscow) by AL Arkov (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) (10.1093/nar/29.19.3982) / Nucleic Acids Res. by A Seit-Nebi (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) (10.1016/S0092-8674(00)80667-4) / Cell by H Song (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) (10.1126/science.289.5481.920) / Science by P Nissen (2000)
  15. Yusupov, M. M. et al. Crystal structure of the ribosome at 5.5 Å resolution. Science 4, 897–902 (2001) / Science by MM Yusupov (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) (10.1093/nar/25.12.2254) / Nucleic Acids Res. by G Drugeon (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) (10.1093/nar/18.22.6537) / Nucleic Acids Res. by WP Tate (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) (10.1038/82818) / Nature Struct. Biol. by KS Wilson (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) (10.1073/pnas.93.11.5443) / Proc. Natl Acad. Sci. USA by K Ito (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) (10.1073/pnas.76.7.3174) / Proc. Natl Acad. Sci. USA by PC Jelenc (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) (10.1006/jsbi.1996.0030) / J. Struct. Biol. by J Frank (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) (10.1006/jmbi.1997.1182) / J. Mol. Biol. by EV Orlova (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) (10.1016/S0092-8674(00)80690-X) / Cell by IS Gabashvili (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) (10.1107/S0108767390010224) / Acta Crystallogr. A by TA Jones (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) (10.1126/science.289.5481.920) / Science by P Nissen (2000)
  26. Wimberly, B. T. et al. Structure of the 30S ribosomal subunit. Nature 407, 327–339 (2000) (10.1038/35030006) / Nature by BT Wimberly (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) (10.1016/S0092-8674(01)00435-4) / Cell by GZ Yusupova (2001)
  28. Carson, M. Ribbons 2.0. J. Appl. Cryst. 24, 103–106 (1991) (10.1107/S0021889891007240) / J. Appl. Cryst. by M Carson (1991)
Dates
Type When
Created 22 years, 7 months ago (Jan. 2, 2003, 12:43 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 2:11 p.m.)
Indexed 2 weeks ago (Aug. 7, 2025, 4:57 p.m.)
Issued 22 years, 7 months ago (Jan. 1, 2003)
Published 22 years, 7 months ago (Jan. 1, 2003)
Published Print 22 years, 7 months ago (Jan. 1, 2003)
Funders 0

None

@article{Rawat_2003, title={A cryo-electron microscopic study of ribosome-bound termination factor RF2}, volume={421}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature01224}, DOI={10.1038/nature01224}, number={6918}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Rawat, Urmila B. S. and Zavialov, Andrey V. and Sengupta, Jayati and Valle, Mikel and Grassucci, Robert A. and Linde, Jamie and Vestergaard, Bente and Ehrenberg, Måns and Frank, Joachim}, year={2003}, month=jan, pages={87–90} }