Protein Quality Control under Oxidative Stress Conditions. Issue 7 (10th April 2015)

• Record Type: Journal Article
• Authors: Dahl, Jan-Ulrik; Gray, Michael J.; Jakob, Ursula
• Is Part Of: Journal of molecular biology. Volume 427:Issue 7(2015:Apr. 01)
• Page Start: 1549
• Page End: 1563
• Publication Date: 2015-04-10
• Subjects: ROS reactive oxygen species -- RCS reactive chlorine species -- Trx thioredoxin -- Grx glutaredoxin -- Gor glutathione oxidoreductase -- GSH glutathione -- HOCl hypochlorous acid -- DUOX dual oxidase -- TA tail-anchored -- RO/CS reactive oxygen and chlorine species; molecular chaperone -- oxidative stress -- protein aggregation -- disulfide bond formation -- N-chlorination; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2015.02.014
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: Accumulation of reactive oxygen and chlorine species (RO/CS) is generally regarded to be a toxic and highly undesirable event, which serves as contributing factor in aging and many age-related diseases. However, it is also put to excellent use during host defense, when high levels of RO/CS are produced to kill invading microorganisms and regulate bacterial colonization. Biochemical and cell biological studies of how bacteria and other microorganisms deal with RO/CS have now provided important new insights into the physiological consequences of oxidative stress, the major targets that need protection, and the cellular strategies employed by organisms to mitigate the damage. This review examines the redox-regulated mechanisms by which cells maintain a functional proteome during oxidative stress. We will discuss the well-characterized redox-regulated chaperone Hsp33, and we will review recent discoveries demonstrating that oxidative stress-specific activation of chaperone function is a much more widespread phenomenon than previously anticipated. New members of this group include the cytosolic ATPase Get3 in yeast, the Escherichia coli protein RidA, and the mammalian protein α2-macroglobulin. We will conclude our review with recent evidence showing that inorganic polyphosphate (polyP), whose accumulation significantly increases bacterial oxidative stress resistance, works by a protein-like chaperone mechanism. Understanding the relationship between oxidative and proteotoxic stresses will improve our understanding of both host–microbe interactions and how mammalian cells combat the damaging side effects of uncontrolled RO/CS production, a hallmark of inflammation. Graphical Abstract: Highlights: Proteome is the major target of oxidative stress in vivo . Proteostasis is maintained by specialized, redox-regulated chaperones. Hsp33 and Get3 are activated by oxidant-induced disulfide bond formation. RidA and α2-macroglobulin are activated by N-chlorination and methionine oxidation. Polyphosphate builds up during oxidative stress and works as protein-like chaperone.