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A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria
Columbia Univ, Dept Chem, 3000 Broadway,MC3126, New York, NY 10027 USA..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Columbia Univ, Dept Chem, 3000 Broadway,MC3126, New York, NY 10027 USA..
2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, article id 1475Article in journal (Refereed) Published
Abstract [en]

Initiation factor (IF) 2 controls the fidelity of translation initiation by selectively increasing the rate of 50S ribosomal subunit joining to 30S initiation complexes (ICs) that carry an N-formyl-methionyl-tRNA (fMet-tRNA(fMet)). Previous studies suggest that rapid 50S subunit joining involves a GTP- and fMet-tRNA(fMet)-dependent "activation" of IF2, but a lack of data on the structure and conformational dynamics of 30S IC-bound IF2 has precluded a mechanistic understanding of this process. Here, using an IF2-tRNA single-molecule fluorescence resonance energy transfer signal, we directly observe the conformational switch that is associated with IF2 activation within 30S ICs that lack IF3. Based on these results, we propose a model of IF2 activation that reveals how GTP, fMet-tRNA(fMet), and specific structural elements of IF2 drive and regulate this conformational switch. Notably, we find that domain III of IF2 plays a pivotal, allosteric, role in IF2 activation, suggesting that this domain can be targeted for the development of novel antibiotics.

Place, publisher, year, edition, pages
2017. Vol. 8, article id 1475
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-342388DOI: 10.1038/s41467-017-01492-6ISI: 000415124000002PubMedID: 29133802OAI: oai:DiVA.org:uu-342388DiVA, id: diva2:1184745
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NIH (National Institute of Health), R01 GM 084288Available from: 2018-02-22 Created: 2018-02-22 Last updated: 2018-02-22Bibliographically approved

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