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J Biol Chem, Vol. 275, Issue 16, 11626-11630, April 21, 2000
From the Laboratoire de Biochimie, Unité Mixte de Recherche
No. 7654, CNRS-Ecole Polytechnique,
91128 Palaiseau Cedex, France
The Saccharomyces cerevisiae YDL219w
(DTD1) gene, which codes for an amino acid sequence sharing
34% identity with the Escherichia coli
D-Tyr-tRNATyr deacylase, was cloned, and its
product was functionally characterized. Overexpression in the yeast of
the DTD1 gene from a multicopy plasmid increased
D-Tyr-tRNATyr deacylase activity in crude
extracts by two orders of magnitude. Upon disruption of the chromosomal
gene, deacylase activity was decreased by more than 90%, and the
sensitivity to D-tyrosine of the growth of S. cerevisiae was exacerbated. The toxicity of D-tyrosine was also enhanced under conditions of nitrogen
starvation, which stimulate the uptake of D-amino acids. In
relation with these behaviors, the capacity of purified S. cerevisiae tyrosyl-tRNA synthetase to produce
D-Tyr-tRNATyr could be shown. Finally, the
phylogenetic distribution of genes homologous to DTD1 was
examined in connection with L-tyrosine prototrophy or
auxotrophy. In the auxotrophs, DTD1-like genes are
systematically absent. In the prototrophs, the putative occurrence of a
deacylase is variable. It possibly depends on the
L-tyrosine anabolic pathway adopted by the cell.
D-Tyrosyl-tRNATyr Metabolism in
Saccharomyces cerevisiae*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: (33) 1 69 33 41 81; Fax: (33) 1 69 33 30 13; E-mail:
plateau@coli.polytechnique.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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