Boyartchuk V L, Rine J
Division of Genetics, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Genetics. 1998 Sep;150(1):95-101. doi: 10.1093/genetics/150.1.95.
In eukaryotes small secreted peptides are often proteolytically cleaved from larger precursors. In Saccharomyces cerevisiae multiple proteolytic processing steps are required for production of mature 12-amino-acid a-factor from its 36-amino-acid precursor. This study provides additional genetic data supporting a direct role for Afc1p in cleavage of the carboxyl-terminal tripeptide from the CAAX motif of the prenylated a-factor precursor. In addition, Afc1p had a second role in a-factor processing that was independent of, and in addition to, its role in the carboxyl-terminal processing in vivo. Using ubiquitin-a-factor fusions we confirmed that the pro-region of the a-factor precursor was not required for production of the mature pheromone. However, the pro-region of the a-factor precursor contributed quantitatively to a-factor production.
在真核生物中,小分泌肽通常从较大的前体经蛋白水解切割产生。在酿酒酵母中,从其36个氨基酸的前体产生成熟的12个氨基酸的a-因子需要多个蛋白水解加工步骤。本研究提供了额外的遗传数据,支持Afc1p在从异戊二烯化的a-因子前体的CAAX基序切割羧基末端三肽中起直接作用。此外,Afc1p在a-因子加工中还有第二个作用,该作用在体内独立于其在羧基末端加工中的作用,且除此之外还有此作用。使用泛素-a-因子融合体,我们证实a-因子前体的前导区对于成熟信息素的产生不是必需的。然而,a-因子前体的前导区对a-因子的产生有定量贡献。