Cloning and sequence of the LYS2 homologue gene from the osmotolerant yeast Pichia sorbitophila.
We have isolated the Pichia sorbitophila LYS2 (PsLYS2) gene by complementation of a lys2 Saccharomyces cerevisiae mutant. The sequenced DNA fragment contains a putative ORF of 4197 bp and the deduced translation product shares a global identity of 66% and 58% to the Lys2 protein homologues of Candida albicans and S. cerevisiae, respectively. Analysis of PsLYS2 sequence suggests that, similarly to S. cerevisiae LYS2, it codes for a polypeptide having two separate enzymatic activities which reside in different domains of the protein, including an adenylate domain, an acyl-carrier site and a short-chain reductase domain. Several GCN4- and NIT2-binding motifs have been matched in the promotor sequence of PsLYS2. In addition, upstream of the sequenced PsLYS2 sequence, we have found the 3'-terminal half of a gene of same orientation encoding a RAD16-like protein, a genomic organization similar to that of C. albicans.
Bleykasten-Grosshans
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Laboratoire de Microbiologie et Génétique, UPRES-A 7010, Université Louis Pasteur/CNRS, 28 rue Goethe, F-67083 Strasbourg, France. bleykasten@gem.u-strasbg.fr
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D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D002176:Candida albicans / Q000201:enzymology / Q000235:genetics; D003001:Cloning, Molecular; D003062:Codon; D005800:Genes, Fungal; D005816:Genetic Complementation Test; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine / Q000096:biosynthesis; D008969:Molecular Sequence Data; D009154:Mutation; D016366:Open Reading Frames; D010843:Pichia / Q000201:enzymology / Q000235:genetics*; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D003062:Codon; D000445:Aldehyde Oxidoreductases; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine