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J Biol Chem, Vol. 274, Issue 27, 19109-19114, July 2, 1999
From the Laboratoire de Biochimie, Unité Mixte de Recherche
No. 7654, CNRS-Ecole Polytechnique,
91128 Palaiseau Cedex, France
The yihZ gene of Escherichia
coli is shown to produce a deacylase activity capable of
recycling misaminoacylated D-Tyr-tRNATyr. The
reaction is specific and, under optimal in vitro
conditions, proceeds at a rate of 6 s
1 with a
Km value for the substrate equal to 1 µM. Cell growth is sensitive to interruption of the
yihZ gene if D-tyrosine is added to minimal
culture medium. Toxicity of exogenous D-tyrosine is
exacerbated if, in addition to the disruption of yihZ, the gene of D-amino acid dehydrogenase (dadA) is
also inactivated. Orthologs of the yihZ gene occur in many,
but not all, bacteria. In support of the idea of a general role of the
D-Tyr-tRNATyr deacylase function in the
detoxification of cells, similar genes can be recognized in
Saccharomyces cerevisiae, Caenorhabditis elegans, Arabidopsis thaliana, mouse, and man.
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