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Crystal structure of the ribosome recycling factor bound to the ribosome
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
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2007 (English)In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 14, no 8, 733-737 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 14, no 8, 733-737 p.
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Biological Sciences
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URN: urn:nbn:se:uu:diva-11588DOI: 10.1038/nsmb1282ISI: 000248555400012PubMedID: 17660830OAI: oai:DiVA.org:uu-11588DiVA: diva2:39357
Note
Forskningen gjord vid MRC Laboratory of Molecular Biology, Cambridge, UK.Available from: 2008-01-30 Created: 2008-01-30 Last updated: 2017-12-11Bibliographically approved

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Selmer, Maria

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