Increased mistranslation protects E. coli from protein misfolding stress due to activation of a RpoS‐dependent heat shock response

The misincorporation of an incorrect amino acid into a polypeptide during protein synthesis is considered a detrimental phenomenon. A mistranslated protein is often misfolded and degraded or nonfunctional and results in an increased cost to quality control machinery. Despite these costs, errors duri...

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Veröffentlicht in:FEBS letters 2019-11, Vol.593 (22), p.3220-3227
Hauptverfasser: Evans, Christopher R., Fan, Yongqiang, Ling, Jiqiang
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Fan, Yongqiang
Ling, Jiqiang
description The misincorporation of an incorrect amino acid into a polypeptide during protein synthesis is considered a detrimental phenomenon. A mistranslated protein is often misfolded and degraded or nonfunctional and results in an increased cost to quality control machinery. Despite these costs, errors during protein synthesis are common in bacteria. Here, we report that mistranslation in Escherichia coli increase the protein level of the heat shock sigma factor RpoH and protect cells against heat stress. Surprisingly, this increase in RpoH due to mistranslation is dependent on the presence of the general stress response sigma factor RpoS. This report provides evidence for a protective function of mistranslation and suggests a novel regulatory role of RpoS in the heat shock response.
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source Wiley Online Library Journals Frontfile Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects heat shock response
mistranslation
Research Letter
Research Letters
RpoH
RpoS
title Increased mistranslation protects E. coli from protein misfolding stress due to activation of a RpoS‐dependent heat shock response
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