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FEBS Lett. 2010 Jul 16;584(14):3055-60. doi: 10.1016/j.febslet.2010.05.036. Epub 2010 May 24.

A bacterial ortholog of class II lysyl-tRNA synthetase activates lysine.

Author information

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. alex.ambrogelly@gmail.com

Abstract

Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs, essential substrates for accurate protein synthesis. Beyond their central role in translation some of these enzymes or their orthologs are recruited for alternative functions, not always related to their primary cellular role. We investigate here the enzymatic properties of GenX (also called PoxA and YjeA), an ortholog of bacterial class II lysyl-tRNA synthetase. GenX is present in most Gram-negative bacteria and is homologous to the catalytic core of lysyl-tRNA synthetase, but it lacks the amino terminal anticodon binding domain of the latter enzyme. We show that, in agreement with its well-conserved lysine binding site, GenX can activate in vitro l-lysine and lysine analogs, but does not acylate tRNA(Lys) or other cellular RNAs.

Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

PMID:
20580719
[PubMed - indexed for MEDLINE]
PMCID:
PMC2900529
Free PMC Article

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