MUTANTS OF SACCHAROMYCES-CEREVISIAE DEFECTIVE IN THE FARNESYLATION OF RAS PROTEINS
MUTANTS OF SACCHAROMYCES-CEREVISIAE DEFECTIVE IN THE FARNESYLATION OF RAS PROTEINS
复制标题
DOI：
10.1073/pnas.87.24.9665
复制
发表时间：
1990-12-01
影响因子：
11.1
通讯作者：
TAMANOI, F
中科院分区：
文献类型：
--
作者：
GOODMAN, LE;JUDD, SR;TAMANOI, F
Ras蛋白通过法尼基化进行后修饰。在本研究中，我们确定了酵母细胞的粗可溶性提取物中的活性，其催化法呢基部分从焦磷酸法呢基转移到酵母RAS 2蛋白。具有C-末端Cys-Ali-Ali-Xaa序列（其中Ali是脂肪族氨基酸，Xaa是未指定的C-末端氨基酸）的RAS 2蛋白充当该反应的底物，而具有改变或缺失的Cys-Ali-Ali-Xaa序列的RAS 2蛋白不充当该反应的底物。一个酵母突变体，dpr 1/ram 1，最初分离的Ras加工突变体被证明是有缺陷的法尼基转移酶活性。此外，另一突变体ram 2也存在转移酶活性缺陷。这些结果表明，至少有两个基因，DPR 1/RAM 1和RAM 2，需要在酵母中的法尼基转移酶活性。
Ras proteins are post-translationally modified by farnesylation. In the present investigation, we identified an activity in crude soluble extracts of yeast cells that catalyzes the transfer of a farnestyl moiety from farnesyl pyrophosphate to yeast RAS2 protein. RAS2 proteins having a C-terminal Cys-Ali-Ali-Xaa sequence (where Ali is an aliphatic amino acid and Xaa is the unspecified C-terminal amino acid) served as substrates for this reaction, whereas RAS2 proteins with an altered or deleted Cys-Ali-Ali-Xaa sequence did not. A yeast mutant, dpr1/ram1, originally isolated as a Ras-processing mutant was shown to be defective in farnesyltransferase activity. In additon, another mutant, ram2, also was defective in the transferase activity. These results demonstrate that at least two genes, DPR1/RAM1 and RAM2, are required for the farnesyltransferase activity in yeast.