Different B-Type Methionine Sulfoxide Reductases in Chlamydomonas May Protect the Alga against High-Light, Sulfur-Depletion, or Oxidative Stress

2013 ◽  
Vol 55 (11) ◽  
pp. 1054-1068 ◽  
Author(s):  
Lei Zhao ◽  
Mei Chen ◽  
Dongmei Cheng ◽  
Haomeng Yang ◽  
Yongle Sun ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Methionine Sulfoxide ◽  
High Light ◽  
Methionine Sulfoxide Reductases

scholarly journals Methionine Sulfoxide Reductases Protect against Oxidative Stress in Staphylococcus aureus Encountering Exogenous Oxidants and Human Neutrophils

2013 ◽  
Vol 6 (3) ◽  
pp. 353-364 ◽  
Author(s):  
Yun Yun Pang ◽  
Jamie Schwartz ◽  
Sarah Bloomberg ◽  
Jeffrey M. Boyd ◽  
Alexander R. Horswill ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Staphylococcus Aureus ◽  
Methionine Sulfoxide ◽  
Human Neutrophils ◽  
Methionine Sulfoxide Reductases

scholarly journals Role of Methionine Sulfoxide Reductases A and B of Enterococcus faecalis in Oxidative Stress and Virulence

2010 ◽  
Vol 78 (9) ◽  
pp. 3889-3897 ◽  
Author(s):  
Chen Zhao ◽  
Axel Hartke ◽  
Marilena La Sorda ◽  
Brunella Posteraro ◽  
Jean-Marie Laplace ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Enterococcus Faecalis ◽  
Galleria Mellonella ◽  
Methionine Sulfoxide ◽  
Peritoneal Macrophages ◽  
Infection Model ◽  
Repair Enzymes ◽  
Methionine Sulfoxide Reductases ◽  
Mouse Peritoneal Macrophages

ABSTRACT Methionine sulfoxide reductases A and B are antioxidant repair enzymes that reduce the S- and R-diastereomers of methionine sulfoxides back to methionine, respectively. Enterococcus faecalis, an important nosocomial pathogen, has one msrA gene and one msrB gene situated in different parts of the chromosome. Promoters have been mapped and mutants have been constructed in two E. faecalis strains (strains JH2-2 and V583) and characterized. For both backgrounds, the mutants are more sensitive than the wild-type parents to exposure to H2O2, and in combination the mutations seem to be additive. The virulence of the mutants has been analyzed in four different models. Survival of the mutants inside mouse peritoneal macrophages stimulated with recombinant gamma interferon plus lipopolysaccharide but not in naïve phagocytes is significantly affected. The msrA mutant is attenuated in the Galleria mellonella insect model. Deficiency in either Msr enzyme reduced the level of virulence in a systemic and urinary tract infection model. Virulence was reconstituted in the complemented strains. The combined results show that Msr repair enzymes are important for the oxidative stress response, macrophage survival, and persistent infection with E. faecalis.

scholarly journals Gene Expression and Physiological Role of Pseudomonas aeruginosa Methionine Sulfoxide Reductases during Oxidative Stress

2013 ◽  
Vol 195 (15) ◽  
pp. 3299-3308 ◽  
Author(s):  
A. Romsang ◽  
S. Atichartpongkul ◽  
W. Trinachartvanit ◽  
P. Vattanaviboon ◽  
S. Mongkolsuk
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Pseudomonas Aeruginosa ◽  
Physiological Role ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductases

scholarly journals Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70, during oxidative stress

2015 ◽  
Vol 26 (3) ◽  
pp. 406-419 ◽  
Author(s):  
Praveen Kumar Allu ◽  
Adinarayana Marada ◽  
Yerranna Boggula ◽  
Srinivasu Karri ◽  
Thanuja Krishnamoorthy ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Yeast Cells ◽  
Nucleotide Exchange ◽  
New Paradigm ◽  
Methionine Sulfoxide Reductases ◽  
Mitochondrial Hsp70

Peptide methionine sulfoxide reductases are conserved enzymes that reduce oxidized methionines in protein(s). Although these reductases have been implicated in several human diseases, there is a dearth of information on the identity of their physiological substrates. By using Saccharomyces cerevisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion of mitochondrial MXR2 renders yeast cells more sensitive to oxidative stress than the cytosolic MXR1. Our earlier studies showed that Mge1, an evolutionarily conserved nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70. In the present study, we show that Mxr2 regulates Mge1 by selectively reducing MetO at position 155 and restores the activity of Mge1 both in vitro and in vivo. Mge1 M155L mutant rescues the slow-growth phenotype and aggregation of proteins of mxr2Δ strain during oxidative stress. By identifying the first mitochondrial substrate for Mxrs, we add a new paradigm to the regulation of the oxidative stress response pathway.

scholarly journals The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function

Antioxidants ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 191 ◽  
Author(s):  
Sofia Lourenço dos Santos ◽  
Isabelle Petropoulos ◽  
Bertrand Friguet
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Protein Function ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductase ◽  
Methionine Oxidation ◽  
Oxygen Species ◽  
Sulfenic Acid ◽  
Protein Repair ◽  
Methionine Sulfoxide Reductases

Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated enzymatic repair systems. Oxidation of cysteine first results in either the formation of a disulfide bridge or a sulfenic acid. Sulfenic acid can be converted to disulfide or sulfenamide or further oxidized to sulfinic acid. Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Methionine side chains can also be oxidized by reactive oxygen species. Methionine oxidation, by the addition of an extra oxygen atom, leads to the generation of methionine sulfoxide. Enzymatically catalyzed reduction of methionine sulfoxide is achieved by either methionine sulfoxide reductase A or methionine sulfoxide reductase B, also referred as to the methionine sulfoxide reductases system. This oxidized protein repair system is further described in this review article in terms of its discovery and biologically relevant characteristics, and its important physiological roles in protecting against oxidative stress, in ageing and in regulating protein function.

scholarly journals Spx mediates oxidative stress regulation of the methionine sulfoxide reductases operon in Bacillus subtilis

2008 ◽  
Vol 8 (1) ◽  
pp. 128 ◽  
Author(s):  
CongHui You ◽  
Agnieszka Sekowska ◽  
Olivera Francetic ◽  
Isabelle Martin-Verstraete ◽  
YiPing Wang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Bacillus Subtilis ◽  
Methionine Sulfoxide ◽  
Stress Regulation ◽  
Methionine Sulfoxide Reductases

Erratum to “Protection from oxidative stress by methionine sulfoxide reductases in RPE cells” [Biochem. Biophys. Res. Commun. 334 (2005) 245–253]

2005 ◽  
Vol 337 (4) ◽  
pp. 1353
Author(s):  
Parameswaran G. Sreekumar ◽  
Ram Kannan ◽  
Jennifer Yaung ◽  
Christine K. Spee ◽  
Stephen J. Ryan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Methionine Sulfoxide ◽  
Rpe Cells ◽  
Methionine Sulfoxide Reductases

scholarly journals Methionine Redox Homeostasis in Protein Quality Control

2021 ◽  
Vol 8 ◽  
Author(s):  
Laurent Aussel ◽  
Benjamin Ezraty
Keyword(s):  
Oxidative Stress ◽  
Quality Control ◽  
Protein Function ◽  
Protein Quality ◽  
Redox Homeostasis ◽  
Protein Quality Control ◽  
Methionine Sulfoxide ◽  
Methionine Sulfoxide Reductases ◽  
Methionine Residues ◽  
And Function

Bacteria live in different environments and are subject to a wide variety of fluctuating conditions. During evolution, they acquired sophisticated systems dedicated to maintaining protein structure and function, especially during oxidative stress. Under such conditions, methionine residues are converted into methionine sulfoxide (Met-O) which can alter protein function. In this review, we focus on the role in protein quality control of methionine sulfoxide reductases (Msr) which repair oxidatively protein-bound Met-O. We discuss our current understanding of the importance of Msr systems in rescuing protein function under oxidative stress and their ability to work in coordination with chaperone networks. Moreover, we highlight that bacterial chaperones, like GroEL or SurA, are also targeted by oxidative stress and under the surveillance of Msr. Therefore, integration of methionine redox homeostasis in protein quality control during oxidative stress gives a complete picture of this bacterial adaptive mechanism.

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