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    Mechanism of premature translation termination on a sense codon

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    J._Biol._Chem._2018_Svidritski ...
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    Authors
    Svidritskiy, Egor
    Demo, Garbriel
    Korostelev, Andrei A.
    UMass Chan Affiliations
    RNA Therapeutics Institute
    Document Type
    Journal Article
    Publication Date
    2018-06-25
    Keywords
    translation release factor
    translation regulation
    ribosome structure
    ribosome function
    RNA–protein interaction
    70S ribosome
    hot-spot sense codon
    hydrophobic interactions
    near-stop codon
    Biochemistry
    Structural Biology
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    Link to Full Text
    https://doi.org/10.1074/jbc.AW118.003232
    Abstract
    Accurate translation termination by release factors (RFs) is critical for the integrity of cellular proteomes. Premature termination on sense codons, for example, results in truncated proteins, whose accumulation could be detrimental to the cell. Nevertheless, some sense codons are prone to triggering premature termination, but the structural basis for this is unclear. To investigate premature termination, we determined a cryo-EM structure of the Escherichia coli 70S ribosome bound with RF1 in response to a UAU (Tyr) sense codon. The structure reveals that RF1 recognizes a UAU codon similarly to a UAG stop codon, suggesting that sense codons induce premature termination because they structurally mimic a stop codon. Hydrophobic interaction between the nucleobase of U3 (the third position of the UAU codon) and conserved Ile 196 in RF1 is important for misreading the UAU codon. Analyses of RNA binding in ribonucleoprotein complexes or by amino acids reveal that Ile-U packing is a frequent protein-RNA binding motif with key functional implications. We discuss parallels with eukaryotic translation termination by the release factor eRF1.
    Source

    J Biol Chem. 2018 Jun 25. pii: AW118.003232. doi: 10.1074/jbc.AW118.003232. Link to article on publisher's site

    DOI
    10.1074/jbc.AW118.003232
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/48824
    PubMed ID
    29941456
    Related Resources

    Link to Article in PubMed

    Rights
    © 2018 Svidritskiy et al. Publisher PDF posted after 12 months as allowed by the publisher's author rights policy at http://www.jbc.org/site/misc/edpolicy.xhtml#copyright.
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.AW118.003232
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