RNA Therapeutics Institute; Department of Biochemistry and Molecular Pharmacology
Biochemistry, Biophysics, and Structural Biology | Cell and Developmental Biology | Genetics and Genomics | Therapeutics
Translation of genetic information encoded in messenger RNAs into polypeptide sequences is carried out by ribosomes in all organisms. When a full protein is synthesized, a stop codon positioned in the ribosomal A site signals termination of translation and protein release. Translation termination depends on class I release factors. Recently, atomic-resolution crystal structures were determined for bacterial 70S ribosome termination complexes bound with release factors RF1 or RF2. In combination with recent biochemical studies, the structures resolve long-standing questions about translation termination. They bring insights into the mechanisms of recognition of all three stop codons, peptidyl-tRNA hydrolysis, and coordination of stop-codon recognition with peptidyl-tRNA hydrolysis. In this review, the structural aspects of these mechanisms are discussed.
70S ribosome, RF1, RF2, crystal structures, release factors
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Copyright © 2011 RNA Society. Freely available online through the RNA Open Access option. Publisher pdf posted as allowed by the publisher's author rights policy at http://rnajournal.cshlp.org/site/misc/terms.xhtml.
DOI of Published Version
RNA. 2011 Aug;17(8):1409-21. doi: 10.1261/rna.2733411. Epub 2011 Jun 23. Link to article on publisher's site
RNA (New York, N.Y.)
Korostelev, Andrei A., "Structural aspects of translation termination on the ribosome" (2011). RNA Therapeutics Institute Publications. 33.