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    Structural aspects of translation termination on the ribosome

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    Authors
    Korostelev, Andrei A.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    RNA Therapeutics Institute
    Document Type
    Journal Article
    Publication Date
    2011-08-01
    Keywords
    70S ribosome
    RF1
    RF2
    crystal structures
    release factors
    Biochemistry, Biophysics, and Structural Biology
    Cell and Developmental Biology
    Genetics and Genomics
    Therapeutics
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153966/
    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.
    Source

    RNA. 2011 Aug;17(8):1409-21. doi: 10.1261/rna.2733411. Epub 2011 Jun 23. Link to article on publisher's site

    DOI
    10.1261/rna.2733411
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/48823
    PubMed ID
    21700725
    Related Resources

    Link to Article in PubMed

    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.
    ae974a485f413a2113503eed53cd6c53
    10.1261/rna.2733411
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