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- Title
A bacterial ortholog of class II lysyl-tRNA synthetase activates lysine
- Authors
Ambrogelly, Alexandre; O’Donoghue, Patrick; Söll, Dieter; Moses, Sarath
- Abstract
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 tRNALys or other cellular RNAs.
- Subjects
AMINOACYL-tRNA synthetases; LYSYL-tRNA synthetase; LYSINE; PROTEIN synthesis; BINDING sites; GENETIC translation
- Publication
FEBS Letters, 2010, Vol 584, Issue 14, p3055
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2010.05.036