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J. Biol. Chem., Vol. 279, Issue 41, 42560-42565, October 8, 2004
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From the Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, 91128 Palaiseau Cedex, France
D-Tyr-tRNATyr deacylase cleaves the ester bond between a tRNA molecule and a D-amino acid. In Escherichia coli, inactivation of the gene (dtd) encoding this deacylase increases the toxicity of several D-amino acids including D-tyrosine, D-tryptophan, and D-aspartic acid. Here, we demonstrate that, in a
dtd cell grown in the presence of 2.4 mM D-tyrosine,
40% of the total tRNATyr pool is converted into D-Tyr-tRNATyr. No D-Tyr-tRNATyr is observed in dtd+ cells. In addition, we observe that overproduction of tRNATyr, tRNATrp, or tRNAAsp protects a
dtd mutant strain against the toxic effect of D-tyrosine, D-tryptophan, or D-aspartic acid, respectively. In the case of D-tyrosine, we show that the protection is accounted for by an increase in the concentration of L-Tyr-tRNATyr proportional to that of overproduced tRNATyr. Altogether, these results indicate that, by accumulating in vivo, high amounts of D-Tyr-tRNATyr cause a starvation for L-Tyr-tRNATyr. The deacylase prevents the starvation by hydrolyzing D-Tyr-tRNATyr. Overproduction of tRNATyr also relieves the starvation by increasing the amount of cellular L-Tyr-tRNATyr available for translation.
Received for publication, March 16, 2004 , and in revised form, July 28, 2004.
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Present address: Laboratoire de Physiologie et Génomique des Cellules Rénales, UMR 7134 CNRS-Paris 6, 15 rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France.
Present address: Service de Biochimie et de Génétique Moléculaire, B
timent 144, CEA/Saclay, 91191 Gif-sur-Yvette Cedex, France.
¶ To whom correspondence should be addressed. Tel.: 33-1-69-33-41-81; Fax: 33-1-69-33-30-13; E-mail: plateau{at}botrytis.polytechnique.fr.
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