ArticleThe Journal of biological chemistry2012
Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 82 citations in OpenAlex.
- One Stone Two Birds: Novel Fluorescent Probe Chemistry That Detects Redox Stress in Cell Culture.Analytical chemistry · 2026Article
- Chiral methionine oxidation reagents reveal stereospecific proteome modifications.bioRxiv : the preprint server for biology · 2026Article
- Antioxidant role of methionine-containing intra- and extracellular proteins.Biophysical reviews · 2023Review
- Discovery and Rational Mutagenesis of Methionine Sulfoxide Reductase Biocatalysts To Expand the Substrate Scope of the Kinetic Resolution of Chiral Sulfoxides.ACS catalysis · 2023Article
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- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- Role of Selenium in Viral Infections with a Major Focus on SARS-CoV-2.International journal of molecular sciences · 2021Review
- Methionine Sulfoxide Reductases Contribute to Anaerobic Fermentative Metabolism inAntioxidants (Basel, Switzerland) · 2021Article
- Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021Review
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- S-methyl-L-cysteine Protects against Antimycin A-induced Mitochondrial Dysfunction in Neural Cells via Mimicking Endogenous Methionine-centered Redox Cycle.Current medical science · 2020Article
- Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020Article
- Role of DJ-1 in Modulating Glycative Stress in Heart Failure.Journal of the American Heart Association · 2020Article
- Addressing Ligand-Based Redox in Molybdenum-Dependent Methionine Sulfoxide Reductase.Journal of the American Chemical Society · 2020Article
- Top-Down Characterization of an Antimicrobial Sanitizer, Leading From Quenchers of Efficacy to Mode of Action.Frontiers in microbiology · 2020Article
- Mitochondrial-targeted methionine sulfoxide reductase overexpression increases the production of oxidative stress in mitochondria from skeletal muscle.Aging pathobiology and therapeutics · 2020Article
- Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2018Review
- Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins.Antioxidants (Basel, Switzerland) · 2018Review
- A conserved R type Methionine Sulfoxide Reductase reverses oxidized GrpEL1/Mge1 to regulate Hsp70 chaperone cycle.Scientific reports · 2018Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Reduction of methionine sulfoxide (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), which act in a stereospecific manner. Catalytic properties of these enzymes were previously established mostly using low molecular weight MetO-containing compounds, whereas little is known about the catalysis of MetO reduction in proteins, the physiological substrates of MSRA and MSRB. In this work we exploited an NADPH-dependent thioredoxin system and determined the kinetic parameters of yeast MSRA and MSRB using three different MetO-containing proteins. Both enzymes showed Michaelis-Menten kinetics with the K(m) lower for protein than for small MetO-containing substrates. MSRA reduced both oxidized proteins and low molecular weight MetO-containing compounds with similar catalytic efficiencies, whereas MSRB was specialized for the reduction of MetO in proteins. Using oxidized glutathione S-transferase as a model substrate, we showed that both MSR types were more efficient in reducing MetO in unfolded than in folded proteins and that their activities increased with the unfolding state. Biochemical quantification and identification of MetO reduced in the substrates by mass spectrometry revealed that the increased activity was due to better access to oxidized MetO in unfolded proteins; it also showed that MSRA was intrinsically more active with unfolded proteins regardless of MetO availability. Moreover, MSRs most efficiently protected cells from oxidative stress that was accompanied by protein unfolding. Overall, this study indicates that MSRs serve a critical function in the folding process by repairing oxidatively damaged nascent polypeptides and unfolded proteins.
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