Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
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DOI：
10.1126/science.275.5307.1796
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发表时间：
1997-03-21
期刊：
影响因子：
56.9
通讯作者：
Rine, J
中科院分区：
文献类型：
--
作者：
Boyartchuk, VL;Ashby, MN;Rine, J
异戊二烯化蛋白质在其羧基末端附近含有共价连接的胆固醇中间体。大多数异戊二烯化蛋白质的成熟涉及最后三个氨基酸的蛋白水解去除。酿酒酵母中的两个基因 RCE1 和 AFC1 被鉴定出负责这种处理。Afc1 蛋白是一种锌蛋白酶，参与酵母 a 因子交配信息素的处理。 Reel 蛋白有助于 Ras 蛋白和 a 因子的加工。 AFC1 和 RCE1 的缺失导致异戊二烯化蛋白质的蛋白水解加工丧失。 RCE1 的破坏导致 Ras 定位和信号传导缺陷，并抑制与等位基因 RAS2(val19) 相关的激活表型。
Prenylated proteins contain a covalently linked cholesterol intermediate near their carboxyl-termini. Maturation of most prenylated proteins involves proteolytic removal of the last three amino acids. Two genes in Saccharomyces cerevisiae, RCE1 and AFC1, were identified that appear to be responsible for this processing, The Afc1 protein is a zinc protease that participates in the processing of yeast a-factor mating pheromone. The Reel protein contributes to the processing of both Ras protein and a-factor. Deletion of both AFC1 and RCE1 resulted in the loss of proteolytic processing of prenylated proteins. Disruption of RCE1 led to defects in Ras localization and signaling and suppressed the activated phenotype associated with the allele RAS2(val19).