SECA PROTEIN HYDROLYZES ATP AND IS AN ESSENTIAL COMPONENT OF THE PROTEIN TRANSLOCATION ATPASE OF ESCHERICHIA-COLI
SECA PROTEIN HYDROLYZES ATP AND IS AN ESSENTIAL COMPONENT OF THE PROTEIN TRANSLOCATION ATPASE OF ESCHERICHIA-COLI
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DOI：
10.1002/j.1460-2075.1989.tb03458.x
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发表时间：
1989-03-01
期刊：
影响因子：
11.4
通讯作者：
WICKNER, W
中科院分区：
文献类型：
--
作者：
LILL, R;CUNNINGHAM, K;WICKNER, W
细菌蛋白质输出需要两种形式的能量输入，ATP和膜电化学电位。使用纯化的可溶性和外周膜成分重建的体外反应，我们现在可以直接测量ATP的易位偶联水解。这种转运ATP酶需要内膜囊泡、SecA蛋白和具有转运能力的proOmpA。膜囊泡的刺激活性可以通过SecY蛋白的抗体或通过从已经在体内非允许温度下孵育的SecY-热敏菌株制备膜来阻断。SecA蛋白本身具有多于一个ATP结合位点。8-叠氮基-ATP使SecA的proOmpA易位和易位ATP酶失活，但不抑制分离的SecA蛋白中固有的低水平ATP水解。这些数据表明SecA蛋白在ATP水解与分泌前蛋白跨膜转移的偶联中具有核心作用。
Bacterial protein export requires two forms of energy input, ATP and the membrane electrochemical potential. Using an in vitro reaction reconstituted with purified soluble and peripheral membrane components, we can now directly measure the translocation-coupled hydrolysis of ATP. This translocation ATPase requires inner membrane vesicles, SecA protein and translocation-competent proOmpA. The stimulatory activity of membrane vesicles can be blocked by either antibody to the SecY protein or by preparing the membranes from a secY-thermosensitive strain which had been incubated at the nonpermissive temperature in vivo. The SecA protein itself has more than one ATP binding site. 8-azido-ATP inactivates SecA for proOmpA translocation and for translocation ATPase, yet does not inhibit a low level of ATP hydrolysis inherent in the isolated SecA protein. These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane.