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Nucleic Acids Res. 2015 Feb 18;43(3):1740-8. doi: 10.1093/nar/gku1404. Epub 2015 Jan 10.

Protein mistranslation protects bacteria against oxidative stress.

Author information

1
Department of Microbiology and Molecular Genetics, Medical School, University of Texas Health Science Center, Houston, TX 77030, USA.
2
Department of Genetics, Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
3
Department of Microbiology and Molecular Genetics, Medical School, University of Texas Health Science Center, Houston, TX 77030, USA Graduate School of Biomedical Sciences, Houston, TX 77030, USA.
4
Department of Microbiology and Molecular Genetics, Medical School, University of Texas Health Science Center, Houston, TX 77030, USA Graduate School of Biomedical Sciences, Houston, TX 77030, USA jiqiang.ling@uth.tmc.edu.

Abstract

Accurate flow of genetic information from DNA to protein requires faithful translation. An increased level of translational errors (mistranslation) has therefore been widely considered harmful to cells. Here we demonstrate that surprisingly, moderate levels of mistranslation indeed increase tolerance to oxidative stress in Escherichia coli. Our RNA sequencing analyses revealed that two antioxidant genes katE and osmC, both controlled by the general stress response activator RpoS, were upregulated by a ribosomal error-prone mutation. Mistranslation-induced tolerance to hydrogen peroxide required rpoS, katE and osmC. We further show that both translational and post-translational regulation of RpoS contribute to peroxide tolerance in the error-prone strain, and a small RNA DsrA, which controls translation of RpoS, is critical for the improved tolerance to oxidative stress through mistranslation. Our work thus challenges the prevailing view that mistranslation is always detrimental, and provides a mechanism by which mistranslation benefits bacteria under stress conditions.

PMID:
25578967
PMCID:
PMC4330365
DOI:
10.1093/nar/gku1404
[Indexed for MEDLINE]
Free PMC Article

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