Reducing systems protecting the bacterial cell envelope from oxidative damage

被引:73
作者
Arts, Isabelle S. [1 ,2 ,3 ]
Gennaris, Alexandra [1 ,2 ,3 ]
Collet, Jean-Francois [1 ,2 ,3 ]
机构
[1] WELBIO, B-1200 Brussels, Belgium
[2] Catholic Univ Louvain, Duve Inst, B-1200 Brussels, Belgium
[3] Brussels Ctr Redox Biol, B-1200 Brussels, Belgium
基金
欧洲研究理事会;
关键词
Methionine sulfoxide; DsbG; PilB; Sulfenic acid; Periplasm; DsbD; METHIONINE SULFOXIDE REDUCTASES; PROTEIN-DISULFIDE ISOMERASE; L-ARABINOSE TRANSPORT; PERIPLASMIC SUPEROXIDE-DISMUTASE; SULFENIC ACID FORMATION; N-TERMINAL DOMAIN; ESCHERICHIA-COLI; BOND FORMATION; THIOL PEROXIDASE; NEISSERIA-MENINGITIDIS;
D O I
10.1016/j.febslet.2015.04.057
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Exposure of cells to elevated levels of reactive oxygen species (ROS) damages DNA, membrane lipids and proteins, which can potentially lead to cell death. In proteins, the sulfur-containing residues cysteine and methionine are particularly sensitive to oxidation, forming sulfenic acids and methionine sulfoxides, respectively. The presence of protection mechanisms to scavenge ROS and repair damaged cellular components is therefore essential for cell survival. The bacterial cell envelope, which constitutes the first protection barrier from the extracellular environment, is particularly exposed to the oxidizing molecules generated by the host cells to kill invading microorganisms. Therefore, the presence of oxidative stress defense mechanisms in that compartment is crucial for cell survival. Here, we review recent findings that led to the identification of several reducing pathways protecting the cell envelope from oxidative damage. We focus in particular on the mechanisms that repair envelope proteins with oxidized cysteine and methionine residues and we discuss the major questions that remain to be solved. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1559 / 1568
页数:10
相关论文
共 118 条
[1]   Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori [J].
Alamuri, P ;
Maier, RJ .
MOLECULAR MICROBIOLOGY, 2004, 53 (05) :1397-1406
[2]   Pneumococcal Gene Complex Involved in Resistance to Extracellular Oxidative Stress [J].
Andisi, Vahid Farshchi ;
Hinojosa, Cecilia A. ;
de Jong, Anne ;
Kuipers, Oscar P. ;
Orihuela, Carlos J. ;
Bijlsma, Jetta J. E. .
INFECTION AND IMMUNITY, 2012, 80 (03) :1037-1049
[3]   Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni [J].
Atack, John M. ;
Kelly, David J. .
MICROBIOLOGY-SGM, 2008, 154 :2219-2230
[4]   An Atlas of the Thioredoxin Fold Class Reveals the Complexity of Function-Enabling Adaptations [J].
Atkinson, Holly J. ;
Babbitt, Patricia C. .
PLOS COMPUTATIONAL BIOLOGY, 2009, 5 (10)
[5]   Oxidative protein folding is driven by the electron transport system [J].
Bader, M ;
Muse, W ;
Ballou, DP ;
Gassner, C ;
Bardwell, JCA .
CELL, 1999, 98 (02) :217-227
[6]   Disulfide bonds are generated by quinone reduction [J].
Bader, MW ;
Xie, T ;
Yu, CA ;
Bardwell, JCA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (34) :26082-26088
[7]   Regulation of reactive oxygen species generation in cell signaling [J].
Bae, Yun Soo ;
Oh, Hyunjin ;
Rhee, Sue Goo ;
Do Yoo, Young .
MOLECULES AND CELLS, 2011, 32 (06) :491-509
[8]   Catalytic mechanism of thiol peroxidase from Escherichia coli -: Sulfenic acid formation and overoxidation of essential CYS61 [J].
Baker, LMS ;
Poole, LB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (11) :9203-9211
[9]   A PATHWAY FOR DISULFIDE BOND FORMATION INVIVO [J].
BARDWELL, JCA ;
LEE, JO ;
JANDER, G ;
MARTIN, N ;
BELIN, D ;
BECKWITH, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (03) :1038-1042
[10]   IDENTIFICATION OF A PROTEIN REQUIRED FOR DISULFIDE BOND FORMATION INVIVO [J].
BARDWELL, JCA ;
MCGOVERN, K ;
BECKWITH, J .
CELL, 1991, 67 (03) :581-589