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J. Biol. Chem., Vol. 275, Issue 42, 32535-32542, October 20, 2000

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Metabolism of D-Aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae Cells^*

Julie Soutourina, Pierre Plateau, and Sylvain Blanquet

From the Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, 91128 Palaiseau Cedex, France

In Escherichia coli, tyrosyl-tRNA synthetase is known to esterify tRNA^Tyr with tyrosine. Resulting D-Tyr-tRNA^Tyr can be hydrolyzed by a D-Tyr-tRNA^Tyr deacylase. By monitoring E. coli growth in liquid medium, we systematically searched for other D-amino acids, the toxicity of which might be exacerbated by the inactivation of the gene encoding D-Tyr-tRNA^Tyr deacylase. In addition to the already documented case of D-tyrosine, positive responses were obtained with D-tryptophan, D-aspartate, D-serine, and D-glutamine. In agreement with this observation, production of D-Asp-tRNA^Asp and D-Trp-tRNA^Trp by aspartyl-tRNA synthetase and tryptophanyl-tRNA synthetase, respectively, was established in vitro. Furthermore, the two D-aminoacylated tRNAs behaved as substrates of purified E. coli D-Tyr-tRNA^Tyr deacylase. These results indicate that an unexpected high number of D-amino acids can impair the bacterium growth through the accumulation of D-aminoacyl-tRNA molecules and that D-Tyr-tRNA^Tyr deacylase has a specificity broad enough to recycle any of these molecules. The same strategy of screening was applied using Saccharomyces cerevisiae, the tyrosyl-tRNA synthetase of which also produces D-Tyr-tRNA^Tyr, and which, like E. coli, possesses a D-Tyr-tRNA^Tyr deacylase activity. In this case, inhibition of growth by the various 19 D-amino acids was followed on solid medium. Two isogenic strains containing or not the deacylase were compared. Toxic effects of D-tyrosine and D-leucine were reinforced upon deprivation of the deacylase. This observation suggests that, in yeast, at least two D-amino acids succeed in being transferred onto tRNAs and that, like in E. coli, the resulting two D-aminoacyl-tRNAs are substrates of a same D-aminoacyl-tRNA deacylase.

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