Peptide methionine sulfoxide reductase: Biochemistry and physiological role

Brot, Nathan; Weissbach, Herbert

doi:10.1002/1097-0282(2000)55:4<288::aid-bip1002>3.0.co;2-m

Cited by 100 publications

(70 citation statements)

References 55 publications

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“…Oxidative damage to proteins can virtually affect all amino acids, sulfur-containing amino acids and aromatic amino acids being the most susceptible to oxidation [2] . Interestingly, certain oxidation products of cysteine and methionine are reversible since they can be brought back to the reduced form of the amino acid within proteins by specific enzymatic systems which correspond to oxidized protein repair enzymes [9,10].…”

Section: Reversible and Irreversible Protein Oxidative Damagementioning

confidence: 99%

“…More recently, chaperone-mediated autophagy has also been shown to be activated upon oxidative stress [8]. Beside degradation, certain types of protein oxidative damage affecting sulfur-containing amino acids have been found to be reversible, hence leading to the possibility that some oxidized proteins could be repaired [9,10]. Indeed, several oxidation products of methionine and cysteine, that are among the most susceptible amino acids to oxidative modification, can be reversed by dedicated enzymatic systems.…”

Section: Introductionmentioning

confidence: 99%

“…Indeed, several oxidation products of methionine and cysteine, that are among the most susceptible amino acids to oxidative modification, can be reversed by dedicated enzymatic systems. Thioredoxin/thioredoxin reductase and glutaredoxin/glutathione/ glutathione reductase can reverse the oxidation of disulfide bridges and cysteine sulfenic acids [10], while methionine sulfoxide reductases catalyze the reduction of methionine sulfoxide back to methionine within proteins [9]. An age-related impairment of oxidized protein elimination (i.e., degradation and repair) would therefore be expected to affect intracellular protein homeostasis and to promote accumulation of oxidatively modified protein.…”

Section: Introductionmentioning

confidence: 99%

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Oxidized protein degradation and repair in ageing and oxidative stress

2006

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Cellular ageing is characterized by the accumulation of oxidatively modified proteins which may be due to increased protein damage and/or decreased elimination of oxidized protein.Since the proteasome is in charge of protein turnover and removal of oxidized protein, its fate during ageing and upon oxidative stress has received special attention, and evidence has been provided for an age-related impairment of proteasome function. However, proteins when oxidized at the level of sulfur-containing amino acids can also be repaired. Therefore, the fate of the methionine sulfoxide reductase system during ageing has also been addressed as well as its role in protection against oxidative stress.

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Section: Reversible and Irreversible Protein Oxidative Damagementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Oxidized protein degradation and repair in ageing and oxidative stress

2006

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“…Methionine is oxidized to two diastereoisomers of Met-SO, Met-(S)-SO and Met-(R)-SO, which differ due to the asymmetry of the sulphur atom in the lateral chain (Ezraty et al, 2005). Oxidized methionine residues are repaired by methionine sulphoxide reductases (Msr), of which there are two major types: MsrA is specific for the S isomer and MsrB for the R isomer (Brot et al, 1981(Brot et al, , 1984Sharov et al, 1999;Brot & Weissbach, 2000;Grimaud et al, 2001;Weissbach et al, 2002). MsrA and MsrB are very highly conserved enzymes in both eukaryotes and prokaryotes, but remarkably, even though their substrates are almost identical, these proteins share no similarity at either the sequence or structural levels (Kauffmann et al, 2002;Lowther et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Atack

Kelly

2008

Microbiology

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The microaerophilic food-borne pathogen Campylobacter jejuni is exposed to highly variable oxygen concentrations during its life cycle and employs a variety of protection mechanisms to resist oxidative stress. However, not all of the enzymes that mediate such protection have yet been identified. Two genes in strain NCTC 11168, Cj0637c and Cj1112c, are predicted to encode unrelated methionine sulphoxide reductases, which may repair oxidized methionine residues in proteins and thus contribute to oxidative stress defence. Cj0637 and Cj1112 were overexpressed, purified and shown by a coupled thioredoxin-thioredoxin reductase-NADPH assay to catalyse the stereospecific reduction of the S and R diastereoisomers, respectively, of the model compound methyl p-tolyl sulphoxide. Cj0637 is thus identified as MsrA and Cj1112 as MsrB. The contribution of these enzymes to oxidative and nitrosative stress resistance in C. jejuni was assessed by phenotypic analysis of a set of isogenic msrA, msrB and msrA/B insertion mutants. As RT-PCR data suggested a polar effect on Cj1111c in the msrB mutant, an msrB/ msrB + merodiploid complementation strain was also constructed. The msrA/B strain was severely growth inhibited under standard microaerobic conditions, whereas the msrA and msrB strains grew normally. Agar plate disc diffusion assays showed that all mutants displayed increased sensitivity to hydrogen peroxide, organic peroxide, superoxide, and nitrosative and disulphide stress, but quantitative cell viability assays showed that the msrA/B double mutant was markedly more sensitive to both oxidative and nitrosative stress. All of the stress-sensitivity phenotypes observed for the msrB mutant were restored to wild-type in the msrB/msrB + merodiploid. It is concluded that MsrA and MsrB make a significant contribution to the protection of C. jejuni against oxidative and nitrosative stress.

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“…The addition of one oxygen atom to either lone pair of electrons of the sulfur atom results in the formation of either the S-or R-form of MetO. MetO has been implicated in a variety of disease states, and in some instances the reduction or repair of this oxidation to Met restores the biological and enzymatic function of proteins (2). The reduction of MetO is mediated by several families of methionine sulfoxide reductases (Msr).…”

mentioning

confidence: 99%

Free methionine-( R )-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

Zhi-dong

Johnson

Weissbach

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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129

138

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The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S-and R-forms of MetO repaired by MsrA and MsrB, respectively. Cell extracts from an MsrA ؊ B ؊ knockout of Escherichia coli have several remaining Msr activities. This study has identified an enzyme specific for the free form of Met-(R)-O, fRMsr, through proteomic analysis. The recombinant enzyme exhibits the same substrate specificity and is as active as MsrA family members. E. coli fRMsr is, however, 100-to 1,000-fold more active than non-selenocysteine-containing MsrB enzymes for free Met-(R)-O. The crystal structure of E. coli fRMsr was previously determined, but no known function was assigned. Thus, the function of this protein has now been determined. The structural similarity of the E. coli and yeast proteins suggests that most fRMsrs use three cysteine residues for catalysis and the formation of a disulfide bond to enclose a small active site cavity. This latter feature is most likely a key determinant of substrate specificity. Moreover, E. coli fRMsr is the first GAF domain family member to show enzymatic activity. Other GAF domain proteins substitute the Cys residues and others to specifically bind cyclic nucleotides, chromophores, and many other ligands for signal potentiation. Therefore, Met-(R)-O may represent a signaling molecule in response to oxidative stress and nutrients via the TOR pathway in some organisms. methionine oxidation ͉ methionine sulfoxide reductase

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Peptide methionine sulfoxide reductase: Biochemistry and physiological role

Cited by 100 publications

References 55 publications

Oxidized protein degradation and repair in ageing and oxidative stress

Oxidized protein degradation and repair in ageing and oxidative stress

Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni

Free methionine-( R )-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

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