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

Yuan, Jing; Hohn, Michael J.; Sherrer, R. Lynn; Palioura, Sotiria; Su, Dan; Soell, Dieter

doi:10.1016/j.febslet.2010.05.028

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

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Yuan, J., Hohn, M. J., Sherrer, R. L., Palioura, S., Su, D., & Soell, D. (2010). A tRNA-dependent cysteine biosynthesis enzyme recognizes the selenocysteine-specific tRNA in Escherichia coli. FEBS LETTERS, 584(13), 2857-2861. doi:10.1016/j.febslet.2010.05.028.

Cite as: https://hdl.handle.net/21.11116/0000-000B-EF1C-A

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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.