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Formation of D-tyrosyl-tRNATyr accounts for the toxicity of D-tyrosine toward Escherichia coli.

Abstract : 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 $\Delta$dtd cell grown in the presence of 2.4 mm D-tyrosine, approximately 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 $\Delta$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-tRNATyr 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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Contributor : Denis Roura Connect in order to contact the contributor
Submitted on : Friday, October 1, 2021 - 10:50:24 AM
Last modification on : Tuesday, October 5, 2021 - 1:59:57 PM


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O. Soutourina, J. Soutourina, Sylvain Blanquet, Pierre Plateau. Formation of D-tyrosyl-tRNATyr accounts for the toxicity of D-tyrosine toward Escherichia coli.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2004, 279 (41), pp.42560-5. ⟨10.1074/jbc.M402931200⟩. ⟨hal-00770709⟩



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