PMID:2170023
| Citation |
Hartl, FU, Lecker, S, Schiebel, E, Hendrick, JP and Wickner, W (1990) The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63:269-79 |
|---|---|
| Abstract |
The export of many E. 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 approximately 6 x 10(-8) M) through direct recognition of both the SecB (Kd approximately 2 x 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 approximately 4 x 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. |
| Links | |
| Keywords |
Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Models, Biological; Protein Binding; Protein Precursors/metabolism; Protein Processing, Post-Translational |
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