ArticleThe Journal of biological chemistry2009
Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 91 citations in OpenAlex.
- Exploring the molecular crosstalk between the sex steroids drospirenone and ethinylestradiol with vaginal lactobacilli.Frontiers in microbiology · 2026Article
- Methionine Modulates the Growth and Development of Heat-Stressed Dermal Papilla Cells via the Wnt/β-Catenin Signaling Pathway.International journal of molecular sciences · 2025Article
- Central Carbon Metabolism inJournal of fungi (Basel, Switzerland) · 2024Article
- Screening and In Silico Analyses of the YeastFoods (Basel, Switzerland) · 2024Article
- Oxidative Stress-Mediated Repression of Virulence Gene Transcription and Biofilm Formation as Antibacterial Action ofInternational journal of molecular sciences · 2024Article
- Discovery and Rational Mutagenesis of Methionine Sulfoxide Reductase Biocatalysts To Expand the Substrate Scope of the Kinetic Resolution of Chiral Sulfoxides.ACS catalysis · 2023Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- The Potential of a Protein Model Synthesized Absent of Methionine.Molecules (Basel, Switzerland) · 2022Review
- Construction of synthetic microbial consortia for 2-keto-L-gulonic acid biosynthesis.Synthetic and systems biotechnology · 2022Article
- Deletion of both methionine sulfoxide reductase A and methionine sulfoxide reductase C genes renders Salmonella Typhimurium highly susceptible to hypochlorite stress and poultry macrophages.Molecular biology reports · 2021Article
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- Top-Down Characterization of an Antimicrobial Sanitizer, Leading From Quenchers of Efficacy to Mode of Action.Frontiers in microbiology · 2020Article
- Oxidative folding pathways of bovine milk β-lactoglobulin with odd cysteine residues.FEBS open bio · 2019Article
- Function of the evolutionarily conserved plant methionine-S-sulfoxide reductase without the catalytic residue.Protoplasma · 2018Article
- Expression of the methionine sulfoxide reductase lost during evolution extends Drosophila lifespan in a methionine-dependent manner.Scientific reports · 2018Article
- Monitoring of Methionine Sulfoxide Content and Methionine Sulfoxide Reductase Activity.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Free radical biology & medicine · 2016Article
- Practical guide for dynamic monitoring of protein oxidation using genetically encoded ratiometric fluorescent biosensors of methionine sulfoxide.Methods (San Diego, Calif.) · 2016Review
- Genome-Wide Analysis of Genes Encoding Methionine-Rich Proteins in Arabidopsis and Soybean Suggesting Their Roles in the Adaptation of Plants to Abiotic Stress.International journal of genomics · 2016Article
- The Impact of Non-Enzymatic Reactions and Enzyme Promiscuity on Cellular Metabolism during (Oxidative) Stress Conditions.Biomolecules · 2015Review
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Methionine sulfoxide reductases (Msrs) are oxidoreductases that catalyze thiol-dependent reduction of oxidized methionines. MsrA and MsrB are the best known Msrs that repair methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO) residues in proteins, respectively. In addition, an Escherichia coli enzyme specific for free Met-R-SO, designated fRMsr, was recently discovered. In this work, we carried out comparative genomic and experimental analyses to examine occurrence, evolution, and function of fRMsr. This protein is present in single copies and two mutually exclusive subtypes in about half of prokaryotes and unicellular eukaryotes but is missing in higher plants and animals. A Saccharomyces cerevisiae fRMsr homolog was found to reduce free Met-R-SO but not free Met-S-SO or dabsyl-Met-R-SO. fRMsr was responsible for growth of yeast cells on Met-R-SO, and the double fRMsr/MsrA mutant could not grow on a mixture of methionine sulfoxides. However, in the presence of methionine, even the triple fRMsr/MsrA/MsrB mutant was viable. In addition, fRMsr deletion strain showed an increased sensitivity to oxidative stress and a decreased life span, whereas overexpression of fRMsr conferred higher resistance to oxidants. Molecular modeling and cysteine residue targeting by thioredoxin pointed to Cys(101) as catalytic and Cys(125) as resolving residues in yeast fRMsr. These residues as well as a third Cys, resolving Cys(91), clustered in the structure, and each was required for the catalytic activity of the enzyme. The data show that fRMsr is the main enzyme responsible for the reduction of free Met-R-SO in S. cerevisiae.
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