Structural aspects of translation termination on the ribosome
dc.contributor.author | Korostelev, Andrei A. | |
dc.date | 2022-08-11T08:10:52.000 | |
dc.date.accessioned | 2022-08-23T17:22:48Z | |
dc.date.available | 2022-08-23T17:22:48Z | |
dc.date.issued | 2011-08-01 | |
dc.date.submitted | 2018-05-17 | |
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.issn | 1355-8382 (Linking) | |
dc.identifier.doi | 10.1261/rna.2733411 | |
dc.identifier.pmid | 21700725 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/48823 | |
dc.description.abstract | 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. | |
dc.language.iso | en_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.url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153966/ | |
dc.rights | 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. | |
dc.subject | 70S ribosome | |
dc.subject | RF1 | |
dc.subject | RF2 | |
dc.subject | crystal structures | |
dc.subject | release factors | |
dc.subject | Biochemistry, Biophysics, and Structural Biology | |
dc.subject | Cell and Developmental Biology | |
dc.subject | Genetics and Genomics | |
dc.subject | Therapeutics | |
dc.title | Structural aspects of translation termination on the ribosome | |
dc.type | Journal Article | |
dc.source.journaltitle | RNA (New York, N.Y.) | |
dc.source.volume | 17 | |
dc.source.issue | 8 | |
dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1032&context=rti_pubs&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/rti_pubs/33 | |
dc.identifier.contextkey | 12144468 | |
refterms.dateFOA | 2022-08-23T17:22:48Z | |
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.submissionpath | rti_pubs/33 | |
dc.contributor.department | Department of Biochemistry and Molecular Pharmacology | |
dc.contributor.department | RNA Therapeutics Institute | |
dc.source.pages | 1409-21 |