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Increased mistranslation protects E. coli from protein misfolding stress due to activation of a RpoS‐dependent heat shock response
Author(s) -
Evans Christopher R.,
Fan Yongqiang,
Ling Jiqiang
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13578
Subject(s) - rpos , sigma factor , heat shock protein , escherichia coli , heat shock , microbiology and biotechnology , shock (circulatory) , protein biosynthesis , chemistry , biology , biochemistry , gene , medicine , gene expression , promoter , rna polymerase
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.