Journal
FEBS LETTERS
Volume 584, Issue 13, Pages 2857-2861Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.05.028
Keywords
Aminoacyl-tRNA; Formate dehydrogenase; Selenocysteine; O-phosphoseryl-tRNA(Sec) kinase; Sep-tRNA:Cys-tRNA synthase; Sep-tRNA:Sec-tRNA synthase
Funding
- Alexander von Humboldt Stiftung
- National Institute of General Medical Sciences
- Yale University School of Medicine
- Department of Energy
- National Institute for General Medical Sciences
- National Science Foundation
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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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