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dc.contributor.authorBao, Chen
dc.contributor.authorLoerch, Sarah
dc.contributor.authorLing, Clarence
dc.contributor.authorKorostelev, Andrei A.
dc.contributor.authorGrigorieff, Nikolaus
dc.contributor.authorErmolenko, Dmitri N.
dc.date2022-08-11T08:09:56.000
dc.date.accessioned2022-08-23T16:49:26Z
dc.date.available2022-08-23T16:49:26Z
dc.date.issued2020-05-19
dc.date.submitted2020-06-05
dc.identifier.citation<p>Bao C, Loerch S, Ling C, Korostelev AA, Grigorieff N, Ermolenko DN. mRNA stem-loops can pause the ribosome by hindering A-site tRNA binding. Elife. 2020 May 19;9:e55799. doi: 10.7554/eLife.55799. Epub ahead of print. PMID: 32427100. <a href="https://doi.org/10.7554/eLife.55799">Link to article on publisher's site</a></p>
dc.identifier.issn2050-084X (Linking)
dc.identifier.doi10.7554/eLife.55799
dc.identifier.pmid32427100
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41462
dc.description.abstractAlthough the elongating ribosome is an efficient helicase, certain mRNA stem-loop structures are known to impede ribosome movement along mRNA and stimulate programmed ribosome frameshifting via mechanisms that are not well understood. Using biochemical and single-molecule Forster resonance energy transfer (smFRET) experiments, we studied how frameshift-inducing stem-loops from E. coli dnaX mRNA and the gag-pol transcript of Human Immunodeficiency Virus (HIV) perturb translation elongation. We find that upon encountering the ribosome, the stem-loops strongly inhibit A-site tRNA binding and ribosome intersubunit rotation that accompanies translation elongation. Electron cryo-microscopy (cryo-EM) reveals that the HIV stem-loop docks into the A site of the ribosome. Our results suggest that mRNA stem-loops can transiently escape the ribosome helicase by binding to the A site. Thus, the stem-loops can modulate gene expression by sterically hindering tRNA binding and inhibiting translation elongation.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=32427100&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights© 2020, Bao et al. This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectE. coli
dc.subjectchromosomes
dc.subjectgene expression
dc.subjectmolecular biophysics
dc.subjectstructural biology
dc.subjectBiochemistry
dc.subjectBiophysics
dc.subjectEnzymes and Coenzymes
dc.subjectMolecular Biology
dc.subjectNucleic Acids, Nucleotides, and Nucleosides
dc.subjectStructural Biology
dc.subjectViruses
dc.titlemRNA stem-loops can pause the ribosome by hindering A-site tRNA binding
dc.typeJournal Article
dc.source.journaltitleeLife
dc.source.volume9
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=5259&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/4240
dc.identifier.contextkey17992630
refterms.dateFOA2022-08-23T16:49:26Z
html.description.abstract<p>Although the elongating ribosome is an efficient helicase, certain mRNA stem-loop structures are known to impede ribosome movement along mRNA and stimulate programmed ribosome frameshifting via mechanisms that are not well understood. Using biochemical and single-molecule Forster resonance energy transfer (smFRET) experiments, we studied how frameshift-inducing stem-loops from E. coli dnaX mRNA and the gag-pol transcript of Human Immunodeficiency Virus (HIV) perturb translation elongation. We find that upon encountering the ribosome, the stem-loops strongly inhibit A-site tRNA binding and ribosome intersubunit rotation that accompanies translation elongation. Electron cryo-microscopy (cryo-EM) reveals that the HIV stem-loop docks into the A site of the ribosome. Our results suggest that mRNA stem-loops can transiently escape the ribosome helicase by binding to the A site. Thus, the stem-loops can modulate gene expression by sterically hindering tRNA binding and inhibiting translation elongation.</p>
dc.identifier.submissionpathoapubs/4240
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentRNA Therapeutics Institute
dc.source.pagese55799


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© 2020, Bao et al. This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
Except where otherwise noted, this item's license is described as © 2020, Bao et al. This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.