A NOVEL YEAST MUTANT DEFECTIVE IN THE PROCESSING OF RAS PROTEINS - ASSESSMENT OF THE EFFECT OF THE MUTATION ON PROCESSING STEPS
A NOVEL YEAST MUTANT DEFECTIVE IN THE PROCESSING OF RAS PROTEINS - ASSESSMENT OF THE EFFECT OF THE MUTATION ON PROCESSING STEPS
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DOI：
10.1002/j.1460-2075.1987.tb04742.x
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发表时间：
1987-01-01
期刊：
影响因子：
11.4
通讯作者：
TAMANOI, F
中科院分区：
文献类型：
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作者：
FUJIYAMA, A;MATSUMOTO, K;TAMANOI, F
酿酒酵母的RAS 1和RAS 2蛋白的生物合成涉及加工、脂肪酸酰化和转运至质膜。我们现在报告的突变体，称为dpr1，在这些生物合成事件的缺陷分离。dpr1细胞对生长温度敏感，并显示a细胞特异性的不育表型。使用过量产生RSA 2蛋白的细胞进行以下观察。(i)在dpr 1细胞中，RAS 2蛋白作为前体保留并积累在细胞质中。(ii)在dpr 1细胞的质膜中的RAS 2蛋白质的水平远低于野生型细胞的质膜中的RAS 2蛋白质的水平。(ii)脂肪酸酰化似乎发生在dpr 1细胞中。这些结果表明，dpr1突变的主要影响是在前体蛋白的加工，但不是在他们的脂肪酸酰化。突变体如dpr1对于进一步阐明RAS蛋白的生物合成和转运机制应该是非常宝贵的，并且可能也是一个因素。
Biosynthesis of RAS1 and RAS2 proteins of Saccharomyces cerevisiae involves processing, fatty acid acylation and transport to plasma membranes. We now report the isolation of a mutant, termed dpr1, defective in these biosynthetic events. The dpr1 cells are temperature sensitive for growth and display sterile phenotype specific to a cells. The following observations were made using cells overproducing the RSA2 protein. (i) In the dpr1 cells, the RAS2 proteins remain as precursors and accumulate in the cytoplasm. (ii) The level of the RAS2 proteins in the plasma membrane of the dpr1 cells is much lower than that in the plasma membrane of wild-type cells. (ii) Fatty acid acylation appears to take place in the dpr1 cells. These results suggest that the major effect of the dpr1 mutation is in the processing of the precursor proteins, but not in their fatty acid acylation. Mutants such as dpr1 should be invaluable for further elucidation of the mechanisms of biosynthesis and transport of the RAS proteins, and presumably also a factor.