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A bacterial ortholog of class II lysyl‐tRNA synthetase activates lysine
Author(s) -
Ambrogelly Alexandre,
O'Donoghue Patrick,
Söll Dieter,
Moses Sarath
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.036
Subject(s) - lysine , transfer rna , aminoacyl trna synthetase , biochemistry , enzyme , biology , translation (biology) , amino acyl trna synthetases , amino acid , chemistry , rna , gene , messenger rna
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.