ArticleFEBS letters2010
A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli.
Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022Review
- Indirect Routes to Aminoacyl-tRNA: The Diversity of Prokaryotic Cysteine Encoding Systems.Frontiers in genetics · 2021Article
- Article
- Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity.Journal of molecular biology · 2014Article
- Recoding the genetic code with selenocysteine.Angewandte Chemie (International ed. in English) · 2014Article
- Random mutagenesis identifies factors involved in formate-dependent growth of the methanogenic archaeon Methanococcus maripaludis.Molecular genetics and genomics : MGG · 2013Article
- Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide.The Journal of biological chemistry · 2012Article
- Mutational analysis of Sep-tRNA:Cys-tRNA synthase reveals critical residues for tRNA-dependent cysteine formation.FEBS letters · 2012Article
- Genetic analysis of selenocysteine biosynthesis in the archaeon Methanococcus maripaludis.Molecular microbiology · 2011Article
- An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions.The Journal of biological chemistry · 2011Article
- An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea.BMC evolutionary biology · 2011Article
- Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea.Archaea (Vancouver, B.C.) · 2010Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The essential methanogen enzyme Sep-tRNA:Cys-tRNA synthase (SepCysS) converts O-phosphoseryl-tRNA(Cys) (Sep-tRNA(Cys)) into Cys-tRNA(Cys) in the presence of a sulfur donor. Likewise, Sep-tRNA:Sec-tRNA synthase converts O-phosphoseryl-tRNA(Sec) (Sep-tRNA(Sec)) to selenocysteinyl-tRNA(Sec) (Sec-tRNA(Sec)) using a selenium donor. While the Sep moiety of the aminoacyl-tRNA substrates is the same in both reactions, tRNA(Cys) and tRNA(Sec) differ greatly in sequence and structure. In an Escherichia coli genetic approach that tests for formate dehydrogenase activity in the absence of selenium donor we show that Sep-tRNA(Sec) is a substrate for SepCysS. Since Sec and Cys are the only active site amino acids known to sustain FDH activity, we conclude that SepCysS converts Sep-tRNA(Sec) to Cys-tRNA(Sec), and that Sep is crucial for SepCysS recognition.
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Registered trials
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