Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase.
We have isolated a mutant which exhibits partial constitutivity for a-specific gene expression in alpha cells. The wild-type gene was cloned and demonstrated to be allelic to the STE13 gene, which encodes the dipeptidyl aminopeptidase involved in processing of the alpha-factor prepropheromone. Thus, the mating defect of the ste13 mutations in alpha cells may result both from the production of incompletely processed alpha-factor and from the increased expression of a-specific genes. The STE13 open reading frame of 931 amino acids contains a putative membrane-spanning segment near its amino terminus and is 31% identical to a second yeast dipeptidyl aminopeptidase (DAP2). A null mutant of STE13 has been constructed: it is viable and sporulation-proficient.
Graduate Group in Genetics, University of California, Berkeley 94720.
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Anna-Arriola
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Herskowitz
D000595:Amino Acid Sequence; D001483:Base Sequence; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000235:genetics*; D005800:Genes, Fungal; D000072235:Mating Factor; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides; D010675:Pheromones / Q000096:biosynthesis*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins
D010455:Peptides; D010675:Pheromones; D029701:Saccharomyces cerevisiae Proteins; D000072235:Mating Factor; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C061833:STE13 protein, S cerevisiae