Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability.
Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability.
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DOI：
10.1093/genetics/146.3.849
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发表时间：
1997-07
期刊：
影响因子：
3.3
通讯作者：
M. Hoyt;J. Macke;B. Roberts;R. Geiser
中科院分区：
文献类型：
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作者：
M. Hoyt;J. Macke;B. Roberts;R. Geiser
酿酒酵母菌CIN1、CIN2和CIN4基因的产物参与正常微管功能所需的非必需途径。在本文中，我们证明了PAC2的产物也在这一途径中起作用。PAC2缺失突变体表现出与cin1 delta、cin2 delta和cin4 delta相似的表型和遗传相互作用。这些包括冷敏感的微管结构和对微管解聚剂苯甲酰的敏感性。所有双突变体重组都是可行的，并且没有比任何单突变体更受影响，这表明参与了一个共同的功能途径。此外，发现额外的CIN1拷贝抑制pac2 delta， cin2 delta和cin4 delta的苯甲酰基敏感性，但不影响其他影响微管功能的突变引起的敏感性。发现Cin1p和Pac2p在序列上与哺乳动物蛋白相关，这些蛋白有助于将β -微管蛋白折叠成具有组装能力的状态。CIN1的等位基因能够以高度特异性的方式抑制cin4-4的苯甲酰基敏感性。我们的研究结果表明，鸟嘌呤核苷酸结合的Cin4p与Cin1p相互作用并调节其微管蛋白折叠活性。
The products of the Saccharomyces cerevisiae CIN1, CIN2 and CIN4 genes participate in a nonessential pathway required for normal microtubule function. In this article, we demonstrate that the product of PAC2 also functions in this pathway. PAC2 deletion mutants displayed phenotypes and genetic interactions similar to those caused by cin1 delta, cin2 delta and cin4 delta. These include cold-sensitive microtubule structures and sensitivity to the microtubule depolymerizing agent benomyl. Involvement in a common functional pathway is indicated by the observation that all double mutant recombinations are viable and no more affected than any single mutant. In addition, extra copies of CIN1 were found to suppress the benomyl sensitivity of pac2 delta, cin2 delta and cin4 delta, but not that caused by other mutations that affect microtubule function. Cin1p and Pac2p were found to be related in sequence to mammalian proteins that aid in the folding of beta-tubulin into an assembly-competent state. Alleles of CIN1 were identified that could suppress the benomyl sensitivity of cin4-4 in a highly specific fashion. Our findings suggest that the guanine nucleotide-binding Cin4p interacts with Cin1p and regulates its tubulin folding activity.