Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon

Sabine Petry, Ditlev E. Brodersen, Frank V. Murphy IV, Christine M. Dunham, Maria Selmer, Michael J. Tarry, Ann C. Kelley, V. Ramakrishnan

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183 Scopus citations

Abstract

During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 Å and 6.7 Å, respectively. The structures reveal details of interactions of the factors with the ribosome and mRNA, including elements previously implicated in decoding and peptide release. They also shed light on conformational changes both in the factors and in the ribosome during termination. Differences seen in the interaction of RF1 and RF2 with the L11 region of the ribosome allow us to rationalize previous biochemical data. Finally, this work demonstrates the feasibility of crystallizing ribosomes with bound factors at a defined state along the translational pathway.

Original languageEnglish (US)
Pages (from-to)1255-1266
Number of pages12
JournalCell
Volume123
Issue number7
DOIs
StatePublished - Dec 29 2005

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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    Petry, S., Brodersen, D. E., Murphy IV, F. V., Dunham, C. M., Selmer, M., Tarry, M. J., Kelley, A. C., & Ramakrishnan, V. (2005). Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon. Cell, 123(7), 1255-1266. https://doi.org/10.1016/j.cell.2005.09.039