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J Biol Chem, Vol. 275, Issue 19, 14056-14063, May 12, 2000

Polyglutamylation of Folate Coenzymes Is Necessary for Methionine Biosynthesis and Maintenance of Intact Mitochondrial Genome in Saccharomyces cerevisiae*

Hélène Cherest, Dominique Thomas, and Yolande Surdin-KerjanDagger

From the Centre de Génétique Moléculaire CNRS 91198 Gif-sur-Yvette cedex, France

One-carbon metabolism is essential to provide activated one-carbon units in the biosynthesis of methionine, purines, and thymidylate. The major forms of folates in vivo are polyglutamylated derivatives. In organisms that synthesize folate coenzymes de novo, the addition of the glutamyl side chains is achieved by the action of two enzymes, dihydrofolate synthetase and folylpolyglutamate synthetase. We report here the characterization and molecular analysis of the two glutamate-adding enzymes of Saccharomyces cerevisiae. We show that dihydrofolate synthetase catalyzing the binding of the first glutamyl side chain to dihydropteroate yielding dihydrofolate is encoded by the YMR113w gene that we propose to rename FOL3. Mutant cells bearing a fol3 mutation require folinic acid for growth and have no dihydrofolate synthetase activity. We show also that folylpolyglutamate synthetase, which catalyzes the extention of the glutamate chains of the folate coenzymes, is encoded by the MET7 gene. Folylpolyglutamate synthetase activity is required for methionine synthesis and for maintenance of mitochondrial DNA. We have tested whether two folylpolyglutamate synthetases could be encoded by the MET7 gene, by the use of alternative initiation codons. Our results show that the loss of mitochondrial functions in met7 mutant cells is not because of the absence of a mitochondrial folylpolyglutamate synthetase.

* This work was supported by the Centre National de la Recherche Scientifique and the Association de la Recherche sur le Cancer.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.

Dagger To whom correspondence should be addressed. Tel.: 33 1 69 82 31 76; Fax: 33 1 69 82 43 72; E-mail: kerjan@cgm.cnrs-gif.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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