Escherichia coli SecB protein associates with exported protein precursors in vivo.
Escherichia coli SecB protein associates with exported protein precursors in vivo.
复制标题
大肠杆菌 SecB 蛋白与体内输出的蛋白前体相关。
DOI：
10.1073/pnas.86.14.5320
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发表时间：
1989
影响因子：
11.1
通讯作者：
Kumamoto,CA
中科院分区：
文献类型：
--
作者：
Kumamoto,CA
大肠杆菌secB基因的产物是跨细胞质膜有效输出蛋白质所必需的。本报告中描述的研究表明，在野生型生长细胞中，SecB蛋白与输出蛋白的前体形式相关联，例如周质麦芽糖结合蛋白（MBP）和外膜蛋白LamB和OmpA。与此相反，细胞质蛋白β-半乳糖苷酶没有发现与SecB。脉冲追踪分析表明，SecB-前体MBP复合物是短暂的，作为一个复杂的，代表了蛋白质输出途径中的中间体预期。这些结果支持SecB蛋白与细胞质中输出的蛋白前体相关联并且在前体跨细胞膜易位之前或期间解离的假设。
The product of the Escherichia coli secB gene is required for efficient export of proteins across the cytoplasmic membrane. The studies described in this report show that in wild-type growing cells, SecB protein associates with precursor forms of exported proteins, such as the periplasmic maltose-binding protein (MBP) and the outer-membrane proteins LamB and OmpA. In contrast, the cytoplasmic protein beta-galactosidase was not found in association with SecB. Pulse-chase analysis showed that the SecB-precursor MBP complex was short lived, as expected for a complex that represents an intermediate in the protein-export pathway. The results support the hypothesis that SecB protein associates with exported protein precursors in the cytoplasm and dissociates prior to or during translocation of precursors across the cell membrane.