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J Biol Chem, Vol. 274, Issue 27, 19109-19114, July 2, 1999

Functional Characterization of the D-Tyr-tRNA^Tyr Deacylase from Escherichia coli

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-tRNA^Tyr. The reaction is specific and, under optimal in vitro conditions, proceeds at a rate of 6 s¹ with a K_m 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-tRNA^Tyr 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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