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      Oxidative stress, protein damage and repair in bacteria

      Author(s): , , ,
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      Journal: Nature Reviews Microbiology
      Publisher: Springer Nature

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          Abstract

          Oxidative damage can have a devastating effect on the structure and activity of proteins, leading to cell death. This Review discusses how bacteria repair oxidized proteins and highlights the importance of these repair systems in physiology and virulence.

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          Critical Review of rate constants for reactions of hydrated electronsChemical Kinetic Data Base for Combustion Chemistry. Part 3: Propane

          George V. Buxton, Clive L. Greenstock, W. Phillips Helman … (1988)
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            Activation of the OxyR transcription factor by reversible disulfide bond formation.

            M Zheng, F Aslund, G Storz (1998)
            The OxyR transcription factor is sensitive to oxidation and activates the expression of antioxidant genes in response to hydrogen peroxide in Escherichia coli. Genetic and biochemical studies revealed that OxyR is activated through the formation of a disulfide bond and is deactivated by enzymatic reduction with glutaredoxin 1 (Grx1). The gene encoding Grx1 is regulated by OxyR, thus providing a mechanism for autoregulation. The redox potential of OxyR was determined to be -185 millivolts, ensuring that OxyR is reduced in the absence of stress. These results represent an example of redox signaling through disulfide bond formation and reduction.
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              Role of oxidative carbonylation in protein quality control and senescence.

              Thomas Nyström (2005)
              Proteins can become modified by a large number of reactions involving reactive oxygen species. Among these reactions, carbonylation has attracted a great deal of attention due to its irreversible and unrepairable nature. Carbonylated proteins are marked for proteolysis by the proteasome and the Lon protease but can escape degradation and form high-molecular-weight aggregates that accumulate with age. Such carbonylated aggregates can become cytotoxic and have been associated with a large number of age-related disorders, including Parkinson's disease, Alzheimer's disease, and cancer. This review focuses on the generation of and defence against protein carbonyls and speculates on the potential role of carbonylation in protein quality control, cellular deterioration, and senescence.
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                Author and article information

                Journal
                Title: Nature Reviews Microbiology
                Abbreviated Title: Nat Rev Micro
                Publisher: Springer Nature
                ISSN (Print): 1740-1526
                ISSN (Electronic): 1740-1534
                Publication date Created: April 19 2017
                Publication date (Print): April 19 2017
                Volume:
                Issue:
                Article
                DOI: 10.1038/nrmicro.2017.26
                PubMed ID: 28420885
                SO-VID: 75c4729c-22c8-46af-ac03-04b54755cea2
                Copyright © © 2017
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