ArticleThe Journal of biological chemistry2012
Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide.
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 8 papers.
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8 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Efficient Sulfide Assimilation in Methanosarcina acetivorans Is Mediated by the MA1715 Protein.Journal of bacteriology · 2016Article
- Interplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway.Biochemistry · 2014Review
- Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The putative tRNA 2-thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis.FEBS letters · 2014Article
- Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis.The Journal of biological chemistry · 2012Article
- Sulfur incorporation into biomolecules: recent advances.Critical reviews in biochemistry and molecular biologyReview
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7 authors at 4 institutions in 1 country.
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Abstract
Sep-tRNA:Cys-tRNA synthase (SepCysS) catalyzes the sulfhydrylation of tRNA-bound O-phosphoserine (Sep) to form cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) in methanogens that lack the canonical cysteinyl-tRNA synthetase (CysRS). A crystal structure of the Archaeoglobus fulgidus SepCysS apoenzyme provides information on the binding of the pyridoxal phosphate cofactor as well as on amino acid residues that may be involved in substrate binding. However, the mechanism of sulfur transfer to form cysteine was not known. Using an in vivo Escherichia coli complementation assay, we showed that all three highly conserved Cys residues in SepCysS (Cys(64), Cys(67), and Cys(272) in the Methanocaldococcus jannaschii enzyme) are essential for the sulfhydrylation reaction in vivo. Biochemical and mass spectrometric analysis demonstrated that Cys(64) and Cys(67) form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. These results suggest that a persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys(272) increased the amount of sulfane sulfur in SepCysS by 3-fold, suggesting that this Cys residue facilitates the generation of the persulfide group. Based upon these findings, we propose for SepCysS a sulfur relay mechanism that recruits both disulfide and persulfide intermediates.
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