在内质网到高尔基体运输过程中GTP结合型Sar1蛋白功能的重建。
Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport.
作者信息
Oka T, Nishikawa S, Nakano A
机构信息
Department of Biology, Faculty of Science, University of Tokyo, Japan.
出版信息
J Cell Biol. 1991 Aug;114(4):671-9. doi: 10.1083/jcb.114.4.671.
Abstract
In the yeast secretory pathway, two genes SEC12 and SAR1, which encode a 70-kD integral membrane protein and a 21-kD GTP-binding protein, respectively, cooperate in protein transport from the ER to the Golgi apparatus. In vivo, the elevation of the SAR1 dosage suppresses temperature sensitivity of the sec12 mutant. In this paper, we show cell-free reconstitution of the ER-to-Golgi transport that depends on both of these gene products. First, the membranes from the sec12 mutant cells reproduce temperature sensitivity in the in vitro ER-to-Golgi transport reaction. Furthermore, the addition of the Sar1 protein completely suppresses this temperature-sensitive defect of the sec12 membranes. The analysis of Sar1p partially purified by E. coli expression suggests that GTP hydrolysis is essential for Sar1p to execute its function.
摘要
在酵母分泌途径中，两个基因SEC12和SAR1分别编码一种70-kD整合膜蛋白和一种21-kD GTP结合蛋白，它们在从内质网到高尔基体的蛋白质运输过程中协同作用。在体内，增加SAR1的剂量可抑制sec12突变体的温度敏感性。在本文中，我们展示了依赖于这两种基因产物的内质网到高尔基体运输的无细胞重建。首先，sec12突变体细胞的膜在体外内质网到高尔基体的运输反应中重现了温度敏感性。此外，添加Sar1蛋白完全抑制了sec12膜的这种温度敏感缺陷。对通过大肠杆菌表达部分纯化的Sar1p的分析表明，GTP水解对于Sar1p执行其功能至关重要。
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