Omer C A, Gibbs J B
Department of Cancer Research, Merck Research Laboratories, West Point, Pennsylvania 19486.
Mol Microbiol. 1994 Jan;11(2):219-25. doi: 10.1111/j.1365-2958.1994.tb00302.x.
Modification of proteins at C-terminal cysteine residue(s) by the isoprenoids farnesyl (C15) and geranylgeranyl (C20) is essential for the biological function of a number of eukaryotic proteins including fungal mating factors and the small, GTP-binding proteins of the Ras superfamily. Three distinct enzymes, conserved between yeast and mammals, have been identified that prenylate proteins: farnesyl protein transferase, geranylgeranyl protein transferase type I and geranylgeranyl protein transferase type II. Each prenyl protein transferase has its own protein substrate specificity. Much has been learned about the biology, genetics and biochemistry of protein prenylation and prenyl protein transferases through studies of eukaryotic microorganisms, particularly Saccharomyces cerevisiae. The functional importance of protein prenylation was first demonstrated with fungal mating factors. The initial genetic analysis of prenyl protein transferases was in S. cerevisiae with the isolation and subsequent characterization of mutations in the RAM1, RAM2, CDC43 and BET2 genes, each of which encodes a prenyl protein transferase subunit. We review here these and other studies on protein prenylation in eukaryotic microbes and how they relate to and have contributed to our knowledge about protein prenylation in all eukaryotic cells.
法尼基（C15）和香叶基香叶基（C20）这两种类异戊二烯对包括真菌交配因子和Ras超家族的小GTP结合蛋白在内的许多真核蛋白的C末端半胱氨酸残基进行蛋白质修饰，对于这些蛋白的生物学功能至关重要。已经鉴定出酵母和哺乳动物中保守的三种不同的酶，它们可将异戊二烯基添加到蛋白质上：法尼基蛋白转移酶、I型香叶基香叶基蛋白转移酶和II型香叶基香叶基蛋白转移酶。每种异戊二烯基蛋白转移酶都有其自身的蛋白质底物特异性。通过对真核微生物，特别是酿酒酵母的研究，人们对蛋白质异戊二烯基化和异戊二烯基蛋白转移酶的生物学、遗传学和生物化学有了很多了解。蛋白质异戊二烯基化的功能重要性最初是通过真菌交配因子得到证明的。异戊二烯基蛋白转移酶的初步遗传分析是在酿酒酵母中进行的，通过分离并随后鉴定RAM1、RAM2、CDC43和BET2基因中的突变，每个基因都编码一个异戊二烯基蛋白转移酶亚基。我们在此回顾这些以及其他关于真核微生物中蛋白质异戊二烯基化的研究，以及它们如何与我们对所有真核细胞中蛋白质异戊二烯基化的认识相关并做出贡献。
