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FEBS Lett. 2010 Jan 21;584(2):272-7. doi: 10.1016/j.febslet.2009.11.085.

Discovery and characterization of tRNAIle lysidine synthetase (TilS).

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1
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan. ts@chembio.t.u-tokyo.ac.jp

Abstract

In the bacterial decoding system, the AUA codon is deciphered as isoleucine by tRNA(Ile) bearing lysidine (L, 2-lysyl-cytidine) at the wobble position. Lysidine is an essential modification that determines both the codon and amino acid specificities of tRNA(Ile). We identified an enzyme named tRNA(Ile) lysidine synthetase (TilS) that catalyzes lysidine formation by using lysine and ATP as substrates. Biochemical studies revealed a molecular mechanism of lysidine formation that consists of two consecutive reactions involving the adenylated tRNA intermediate. In addition, we deciphered how Escherichia coli TilS specifically discriminates between tRNA(Ile) and the structurally similar tRNA(Met), which bears the same anticodon loop. Recent structural studies unveiled tRNA recognition by TilS, and a molecular basis of lysidine formation at atomic resolution.

PMID:
19944692
DOI:
10.1016/j.febslet.2009.11.085
[Indexed for MEDLINE]
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