SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
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DOI：
10.1016/0092-8674(95)90143-4
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发表时间：
1995-12-29
期刊：
影响因子：
64.5
通讯作者：
Wickner, W
中科院分区：
文献类型：
--
作者：
Economou, A;Pogliano, JA;Wickner, W
E.大肠杆菌前蛋白转位酶在SecYEG的膜插入和脱插入循环期间促进蛋白分泌。这一过程受核苷酸结合和水解以及SecD和SecF蛋白的调节。在相关的前蛋白的存在下，ATP结合在核苷酸结合结构域1（NBD1）的能量驱动SecA的30 kDa结构域的膜插入，而SecA的脱插入需要该ATP的水解。SecD和SecF稳定SecA的插入状态。ATP结合NBD 2，虽然需要前蛋白易位，是不需要SecA插入或脱插入。
The SecA subunit of E. coli preprotein translocase promotes protein secretion during cycles of membrane insertion and deinsertion at SecYEG. This process is regulated both by nucleotide binding and hydrolysis and by the SecD and SecF proteins. In the presence of associated preprotein, the energy of ATP binding at nucleotide-binding domain 1 (NBD1) drives membrane insertion of a 30 kDa domain of SecA, while deinsertion of SecA requires the hydrolysis of this ATP. SecD and SecF stabilize the inserted state of SecA. ATP binding at NBD2, though needed for preprotein translocation, is not needed for SecA insertion or deinsertion.