Formation of D-tyrosyl-tRNATyr accounts for the toxicity of D-tyrosine towards Escherichia coli?

doi:10.1074/jbc.M402931200

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Papers In Press, published online ahead of print August 2, 2004
J. Biol. Chem, 10.1074/jbc.M402931200
Submitted on March 16, 2004
Revised on July 28, 2004
Accepted on August 2, 2004

Formation of D-tyrosyl-tRNA^Tyr accounts for the toxicity of D-tyrosine towards Escherichia coli?

Olga Soutourina, Julie Soutourina, Sylvain Blanquet, and Pierre Plateau

Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau 91128

Corresponding Author: plateau{at}botrytis.polytechnique.fr

D-Tyr-tRNA^Tyr 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 tRNA^Tyr pool is converted into D-Tyr-tRNA^Tyr. No D-Tyr-tRNA^Tyr is observed in dtd⁺ cells. In addition, we observe that overproduction of tRNA^Tyr, tRNA^Trp or tRNA^Asp 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-tRNA^Tyr proportional to that of overproduced tRNA^Tyr. Altogether, these results indicate that, by accumulating in vivo, high amounts of D-Tyr-tRNA^Tyr cause a starvation for L-Tyr-tRNA^Tyr. The deacylase prevents the starvation by hydrolyzing D-Tyr-tRNA^Tyr. Overproduction of tRNA^Tyr also relieves the starvation by increasing the amount of cellular L-Tyr-tRNA^Tyr available for translation.›

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