ArticleThe Journal of biological chemistry2011
A 4-selenocysteine, 2-selenocysteine insertion sequence (SECIS) element methionine sulfoxide reductase from Metridium senile reveals a non-catalytic function of selenocysteines.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025Review
- Silibinin Can Promote Bone Regeneration of Selenium Hydrogel by Reducing the Oxidative Stress Pathway in Ovariectomized Rats.Calcified tissue international · 2022Article
- Lokiarchaeota Marks the Transition between the Archaeal and Eukaryotic Selenocysteine Encoding Systems.Molecular biology and evolution · 2016Article
- Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential.FEBS letters · 2014Article
- Article
- Antibody conjugation via one and two C-terminal selenocysteines.Methods (San Diego, Calif.) · 2014Article
- The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions.Antioxidants & redox signaling · 2013Review
- Selenocysteine in thiol/disulfide-like exchange reactions.Antioxidants & redox signaling · 2013Review
- Analysis and functional prediction of reactive cysteine residues.The Journal of biological chemistry · 2012Review
- Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Advances in microbial physiology · 2012Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Selenocysteine (Sec) residues occur in thiol oxidoreductase families, and functionally characterized selenoenzymes typically have a single Sec residue used directly for redox catalysis. However, how new Sec residues evolve and whether non-catalytic Sec residues exist in proteins is not known. Here, we computationally identified several genes with multiple Sec insertion sequence (SECIS) elements, one of which was a methionine-R-sulfoxide reductase (MsrB) homolog from Metridium senile that has four in-frame UGA codons and two nearly identical SECIS elements. One of the UGA codons corresponded to the conserved catalytic Sec or Cys in MsrBs, whereas the three other UGA codons evolved recently and had no homologs with Sec or Cys in these positions. Metabolic (75)Se labeling showed that all four in-frame UGA codons supported Sec insertion and that both SECIS elements were functional and collaborated in Sec insertion at each UGA codon. Interestingly, recombinant M. senile MsrB bound iron, and further analyses suggested the possibility of binding an iron-sulfur cluster by the protein. These data show that Sec residues may appear transiently in genes containing SECIS elements and be adapted for non-catalytic functions.
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