A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli

被引：17

作者：

Yuan, Jing ^{[1
]}

Hohn, Michael J. ^{[1
]}

Sherrer, R. Lynn ^{[1
]}

Palioura, Sotiria ^{[1
]}

Su, Dan ^{[1
]}

Soell, Dieter ^{[1
,2
]}

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA

来源：

FEBS LETTERS | 2010年 / 584卷 / 13期

基金：

美国国家科学基金会;

关键词：

Aminoacyl-tRNA; Formate dehydrogenase; Selenocysteine; O-phosphoseryl-tRNA(Sec) kinase; Sep-tRNA:Cys-tRNA synthase; Sep-tRNA:Sec-tRNA synthase; ELONGATION-FACTOR SELB; FORMATE DEHYDROGENASE; SALMONELLA-TYPHIMURIUM; STRUCTURAL INSIGHTS; SELENIUM METABOLISM; CRYSTAL-STRUCTURE; SYNTHASE; ARCHAEA; SYNTHETASE; MECHANISM;

D O I：

10.1016/j.febslet.2010.05.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2857 / 2861

页数：5

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