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.[1]References
- Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase. Anna-Arriola, S.S., Herskowitz, I. Yeast (1994) [Pubmed]
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