THE BINDING CASCADE OF SECB TO SECA TO SECY/E MEDIATES PREPROTEIN TARGETING TO THE ESCHERICHIA-COLI PLASMA-MEMBRANE
THE BINDING CASCADE OF SECB TO SECA TO SECY/E MEDIATES PREPROTEIN TARGETING TO THE ESCHERICHIA-COLI PLASMA-MEMBRANE
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DOI:
10.1016/0092-8674(90)90160-g
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发表时间:
1990-10-19
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:
HARTL, FU;LECKER, S;WICKNER, W
The export of many Escherichia coli proteins such as proOmpA requires the cytosolic chaperone SecB and the membrane-bound preprotein translocase. Translocase is a multisubunit enzyme with the SecA protein as its peripheral membrane domain and the SecY/E protein as its integral domain. SecB, by binding to proOmpA in the cytosol, prevents its aggregation or association with membranes at nonproductive sites. The SecA receptor binds the proOmpA-SecB complex (Kd .apprxeq. 6 .times. 10-8 M) through direct recognition of both the SecB (Kd .apprxeq. 2 .times. 10-7 M) as well as the leader and mature domains of the precursor protein. SecB has a dual function in stabilizing the precursor and in passing it on to membrane-bound SecA, the next step in the pathway. SecA itself is bound to the membrane by its affinity (Kd .apprxeq. 4 .times. 10-8 M) for SecY/E and for acidic lipids. The functions of SecB and SecA as a two-stage receptor system are linked by their affinity for each other.