Carboxypeptidase yscS: gene structure and function of the vacuolar enzyme.
The gene encoding carboxypeptidase yscS in Saccharomyces cerevisiae, CPS1, was cloned by complementation of the cps1-3 mutation. The cloned CPS1 gene, which again enabled a leucine auxotrophic cps1-3 mutant to grow on the modified dipeptide Cbz-Gly-Leu (Cbz, benzyloxycarbonyl) as sole leucine source, was sequenced and found to consist of an open reading frame of 1728 bp encoding a protein of 576 amino acids. The putative protein contains a hydrophobic stretch of 20 amino acids and a putative signal sequence cleavage site. Five putative N-glycosylation sites are also in the protein sequence. This data is consistent with the previous finding of carboxypeptidase yscS being a vacuolar peptidase. Chromosomal disruption of the CPS1 gene completely abolishes carboxypeptidase yscS activity. This protein is yet another member of the peptidases in S. cerevisiae involved in nitrogen metabolism.
Spormann
D O
DO
Ciba-Geigy AG, Abteilung Biotechnologie, Basel, Switzerland.
Heim
J
J
Wolf
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DH
D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D015825:Chromosomes, Fungal; D004271:DNA, Fungal / Q000235:genetics; D006031:Glycosylation; D008969:Molecular Sequence Data; D009154:Mutation; D012331:RNA, Fungal / Q000032:analysis; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000254:growth & development; D016385:TATA Box
D004271:DNA, Fungal; D012331:RNA, Fungal; D002268:Carboxypeptidases