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dc.contributor.authorKorostelev, Andrei A.
dc.date2022-08-11T08:10:52.000
dc.date.accessioned2022-08-23T17:22:48Z
dc.date.available2022-08-23T17:22:48Z
dc.date.issued2011-08-01
dc.date.submitted2018-05-17
dc.identifier.citation<p>RNA. 2011 Aug;17(8):1409-21. doi: 10.1261/rna.2733411. Epub 2011 Jun 23. <a href="https://doi.org/10.1261/rna.2733411">Link to article on publisher's site</a></p>
dc.identifier.issn1355-8382 (Linking)
dc.identifier.doi10.1261/rna.2733411
dc.identifier.pmid21700725
dc.identifier.urihttp://hdl.handle.net/20.500.14038/48823
dc.description.abstractTranslation 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=21700725&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153966/
dc.rightsCopyright © 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.
dc.subject70S ribosome
dc.subjectRF1
dc.subjectRF2
dc.subjectcrystal structures
dc.subjectrelease factors
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectCell and Developmental Biology
dc.subjectGenetics and Genomics
dc.subjectTherapeutics
dc.titleStructural aspects of translation termination on the ribosome
dc.typeJournal Article
dc.source.journaltitleRNA (New York, N.Y.)
dc.source.volume17
dc.source.issue8
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1032&amp;context=rti_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/rti_pubs/33
dc.identifier.contextkey12144468
refterms.dateFOA2022-08-23T17:22:48Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathrti_pubs/33
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentRNA Therapeutics Institute
dc.source.pages1409-21


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