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.
Predicate | Object |
---|---|
rdf:type | |
rdfs:comment |
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.
|
skos:exactMatch | |
uniprot:name |
Yeast
|
uniprot:author |
Anna-Arriola S.S.,
Herskowitz I.
|
uniprot:date |
1994
|
uniprot:pages |
801-810
|
uniprot:title |
Isolation and DNA sequence of the STE13 gene encoding dipeptidyl aminopeptidase.
|
uniprot:volume |
10
|
dc-term:identifier |
doi:10.1002/yea.320100610
|