Crystal structure of the ribosome recycling factor bound to the ribosome

Albert Weixlbaumer, Sabine Petry, Christine M. Dunham, Maria Selmer, Ann C. Kelley, V. Ramakrishnan

Research output: Contribution to journalArticle

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Abstract

In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.

Original languageEnglish (US)
Pages (from-to)733-737
Number of pages5
JournalNature Structural and Molecular Biology
Volume14
Issue number8
DOIs
StatePublished - Aug 1 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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    Weixlbaumer, A., Petry, S., Dunham, C. M., Selmer, M., Kelley, A. C., & Ramakrishnan, V. (2007). Crystal structure of the ribosome recycling factor bound to the ribosome. Nature Structural and Molecular Biology, 14(8), 733-737. https://doi.org/10.1038/nsmb1282