Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC.
نویسندگان
چکیده
The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK(2) maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.
منابع مشابه
Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly.
Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK(2) maltose transporter complex both in detergent solution and in proteoliposomes.
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 283 26 شماره
صفحات -
تاریخ انتشار 2008