Abstract
Saccharomyces cerevisiae contains two genes, SAM1 and SAM2, encoding functional S-adenosylmethionine synthetases. The gene SAM1 was isolated by functional complementation of a double mutant of S. cerevisiae, and its identity was confirmed by gene disruption. The cloned gene was used to probe wild type chromosomal DNA, and two regions hybridizing with SAM1 were found, one of which is the SAM1 region. The DNA sequence of SAM1 is reported. The translation product shows a high homology with the one deduced from the sequence of the MetK gene encoding the SAM synthetase of Escherichia coli.
Highlights
Dominique Thomas and Yolande Surdin-Kerjan From the Laboratoire d’Enzymologiedu Centre Nationalde la Recherche Scientifique, 91 190 Gif-sur- Yvette, France
The gene SAMl was isolated by functional complementation of a double mutant of S. cerevisiae, and its identitywas confirmed by gene
In Escherichia coli it has been shown that metK phase cells (1-3X lo6cells/ml) with zymolase60,000at a concentrais the structural gene for AdoMet synthetase
Summary
Dominique Thomas and Yolande Surdin-Kerjan From the Laboratoire d’Enzymologiedu Centre Nationalde la Recherche Scientifique, 91 190 Gif-sur- Yvette, France. SAMl and SAM2, encoding functional S-adenosylmethionine synthetases. The DNA sequence of SAMl is reported. The translation product shows a high homology with the one deduced from the sequence of the MetK gene encoding the SAM synthetase of Escherichia coli. Strain CC359-OL2 (a, ura, his, leu2) was transformed for SAM2 gene disruption. Cerevisiae-RNAs were prepared from strain FLlOO as described previously (Cherest et al, 1985). In Escherichia coli it has been shown that metK phase cells (1-3X lo6cells/ml) with zymolase60,000at a concentrais the structural gene for AdoMet synthetase An E. coli strain cellulosechromatographywereperformedasdescribedpreviously with a transposoninsertionin gene metKshowsresidual except that the buffer for extraction was100 mM potassium phos-. Prior to the DEAE-cellulose columnthe SlOO extract was desalted by filtration on Sephadex G-25as described earlier (Cherest second enzyme (Mulligan et al, 1982).
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