ArticleProteins2009
The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A.
Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 45 citations in OpenAlex.
- Recent advances in exploring the composition and evolution of the prokaryotic selenoproteome.Applied and environmental microbiology · 2026Review
- deep-Sep: a deep learning-based method for fast and accurate prediction of selenoprotein genes in bacteria.mSystems · 2025Article
- Eight Unexpected Selenoprotein Families in Organometallic Biochemistry in Clostridium difficile, in ABC Transport, and in Methylmercury Biosynthesis.Journal of bacteriology · 2023Article
- Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective.Biomolecules · 2022Review
- Methionine Sulfoxide Reductases Contribute to Anaerobic Fermentative Metabolism inAntioxidants (Basel, Switzerland) · 2021Article
- Monothiol and dithiol glutaredoxin-1 fromIUCrJ · 2020Article
- Generation of Recombinant Mammalian Selenoproteins through Genetic Code Expansion with Photocaged Selenocysteine.ACS chemical biology · 2020Article
- Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance.Applied and environmental microbiology · 2015Article
- Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.PloS one · 2015Article
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.PloS one · 2015Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.Antioxidants & redox signaling · 2013Review
- Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.Molecular microbiology · 2011Article
- The biological significance of methionine sulfoxide stereochemistry.Free radical biology & medicine · 2011Review
- General trends in trace element utilization revealed by comparative genomic analyses of Co, Cu, Mo, Ni, and Se.The Journal of biological chemistry · 2010Article
- Recode-2: new design, new search tools, and many more genes.Nucleic acids research · 2010Article
- Functions and evolution of selenoprotein methionine sulfoxide reductases.Biochimica et biophysica acta · 2009Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Selenocysteine (Sec) is incorporated into proteins in response to UGA codons. This residue is frequently found at the catalytic sites of oxidoreductases. In this study, we characterized the selenoproteome of an anaerobic bacterium, Clostridium sp. (also known as Alkaliphilus oremlandii) OhILA, and identified 13 selenoprotein genes, five of which have not been previously described. One of the detected selenoproteins was methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that repairs oxidatively damaged methionines in a stereospecific manner. To date, little is known about MsrA from anaerobes. We characterized this selenoprotein MsrA which had a single Sec residue at the catalytic site but no cysteine (Cys) residues in the protein sequence. Its SECIS (Sec insertion sequence) element did not resemble those in Escherichia coli. Although with low translational efficiency, the expression of the Clostridium selenoprotein msrA gene in E. coli could be demonstrated by (75)Se metabolic labeling, immunoblot analyses, and enzyme assays, indicating that its SECIS element was recognized by the E. coli Sec insertion machinery. We found that the Sec-containing MsrA exhibited at least a 20-fold higher activity than its Cys mutant form, indicating a critical role of Sec in the catalytic activity of the enzyme. Furthermore, our data revealed that the Clostridium MsrA was inefficiently reducible by thioredoxin, which is a typical reducing agent for MsrA, suggesting the use of alternative electron donors in this anaerobic bacterium that directly act on the selenenic acid intermediate and do not require resolving Cys residues.
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