RNA Therapeutics Institute Publications

UMMS Affiliation

RNA Therapeutics Institute; Department of Biochemistry and Molecular Pharmacology

Publication Date


Document Type



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

Rights and Permissions

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

Journal/Book/Conference Title

RNA (New York, N.Y.)

Related Resources

Link to Article in PubMed

PubMed ID




To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.