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酵母α因子是由一种更大的前体多肽加工而来:一种膜结合二肽基氨肽酶的重要作用。

Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase.

作者信息

Julius D, Blair L, Brake A, Sprague G, Thorner J

出版信息

Cell. 1983 Mar;32(3):839-52. doi: 10.1016/0092-8674(83)90070-3.

DOI:10.1016/0092-8674(83)90070-3
PMID:6339075
Abstract

Alpha factor mating pheromone is a peptide of 13 amino acids secreted by Saccharomyces 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 and H2N-AspAlaGluAla-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 tenfold. Other experiments indicate that DPAPase A action may be rate-limiting for alpha-factor maturation in normal alpha cells.

摘要

α因子交配信息素是酿酒酵母α细胞分泌的一种由13个氨基酸组成的肽。在STE13基因中存在缺陷的非交配型(“不育型”,即ste)α细胞突变体不产生正常的α因子,而是释放出一系列加工不完全的形式(α因子),这些形式的比生物活性明显降低。主要的α因子肽具有H2N-GluAlaGluAla-α因子和H2N-AspAlaGluAla-α因子的结构。ste13突变体缺乏一种膜结合的热稳定二肽基氨基肽酶(DPAPase A),该酶特异性地在重复的-X-Ala-序列的羧基侧进行切割。DPAPase A的缺失以及ste13损伤的其他表型在遗传杂交中共同分离。质粒上克隆的STE13基因使酵母细胞过量产生DPAPase A达数倍之多。另一个克隆的DNA片段可微弱抑制ste13缺陷,使一种热不稳定活性(DPAPase B)过量产生约10倍。其他实验表明,在正常α细胞中,DPAPase A的作用可能是α因子成熟的限速因素。

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