YEAST ALPHA-FACTOR IS PROCESSED FROM A LARGER PRECURSOR POLYPEPTIDE - THE ESSENTIAL ROLE OF A MEMBRANE-BOUND DIPEPTIDYL AMINOPEPTIDASE
YEAST ALPHA-FACTOR IS PROCESSED FROM A LARGER PRECURSOR POLYPEPTIDE - THE ESSENTIAL ROLE OF A MEMBRANE-BOUND DIPEPTIDYL AMINOPEPTIDASE
复制标题
DOI:
10.1016/0092-8674(83)90070-3
复制
发表时间:
1983-01-01
期刊:
影响因子:
64.5
通讯作者:
THORNER, J
中科院分区:
文献类型:
--
作者:
JULIUS, D;BLAIR, L;THORNER, J
Alpha factor mating pheromone is a peptide of 13 amino acids secreted by S. cerevisiae .alpha. cells. Nonmating (sterile, or ste) .alpha.-cell mutants bearing defects in the STE13 gene do not produce normal .alpha. factor, but release a collection of incompletely processed forms (.alpha. factor*) that have a markedly reduced specific biological activity. The major .alpha.-factor* peptides have the structures H2N-GluAlaGluAla-.alpha. factor. The ste13 mutants lack a membrane-bound heat-stable dipeptidyl aminopeptidase (DPAPase A) that specifically cleaves on the carboxyl side of repeating -X-Ala- sequences. Absence of DPAPase A and the other phenotypes of a ste13 lesion cosegregate in genetic crosses. The cloned STE13 gene on a plasmid causes yeast cells to overproduce DPAPase A severalfold. A different cloned DNA segment, which weakly suppresses the ste13 defects, causes overproduction of a heat-labile activity (DPAPase B) by about 10-fold. Other experiments indicate that DPAPase A action may be rate-limiting for .alpha.-factor maturation in normal .alpha. cells.