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A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P
Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). Institute of Technology, University of Tartu, Tartu 50090, Estonia.
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2014 (English)In: Cell reports, ISSN 2211-1247, E-ISSN 2211-1247, Vol. 9, no 2, 476-483 p.Article in journal (Refereed) Published
Abstract [en]

Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyproline stretches in proteins. We have discovered that only a single polyproline stretch is invariant across all domains of life, namely a proline triplet in ValS, the tRNA synthetase, that charges tRNA(Val) with valine. Here, we show that expression of ValS in vivo and in vitro requires EF-P and demonstrate that the proline triplet located in the active site of ValS is important for efficient charging of tRNA(Val) with valine and preventing formation of mischarged Thr-tRNA(Val) as well as efficient growth of E. coli in vivo. We suggest that the critical role of the proline triplet for ValS activity may explain why bacterial cells coevolved the EF-P rescue system.

Place, publisher, year, edition, pages
Cell Press , 2014. Vol. 9, no 2, 476-483 p.
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Cell and Molecular Biology
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URN: urn:nbn:se:umu:diva-97232DOI: 10.1016/j.celrep.2014.09.008ISI: 000344469100008PubMedID: 25310979OAI: oai:DiVA.org:umu-97232DiVA: diva2:773219
Available from: 2014-12-18 Created: 2014-12-12 Last updated: 2017-12-05Bibliographically approved

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Atkinson, Gemma C

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CiteExportLink to record
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Citation style
  • apa
  • ieee
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  • Other style
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Language
  • de-DE
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  • nn-NO
  • nn-NB
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  • Other locale
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Output format
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