Phospholipid-assisted refolding of an integral membrane protein - Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone

被引:113
作者
Bogdanov, M
Umeda, M
Dowhan, W
机构
[1] Univ Texas, Sch Med, Dept Biochem & Mol Biol, Houston, TX 77225 USA
[2] Tokyo Metropolitan Inst Med Sci, Dept Mol Biodynam, Tokyo 113, Japan
关键词
D O I
10.1074/jbc.274.18.12339
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Escherichia coli-derived phosphatidylethanolamine (PE) or PE with fully saturated fatty acids was able to correct in vitro a defect in folding in the lipid dependent epitope 4B1 of lactose permease (LacY) resulting from in vivo assembly in the absence of PE. PE plasmalogen, PE with two unsaturated fatty acids, and lyso-PE, which all do not favor bilayer organization, did not support proper refolding, Proper refolding occurred when these latter lipids were mixed with a bilayer-forming lipid (phosphatidylglycerol), which alone could not support refolding, L-Phosphatidylserine (PS; natural diastereomer) did support proper refolding, PE derivatives of increasing degrees of methylation were progressively less effective in supporting refolding, with phosphatidylcholine being completely ineffective. Therefore, the properties of nonmethylated aminophospholipids capable of organization into a bilayer configuration are essential for the recovery of the native state of epitope 4B1 after misassembly in vivo in the absence of PE, Neither D-PS (sn-glycero-l-phosphate backbone) nor P-D-S (D-serine in the head group) is competent in supporting proper refolding unless used in binary mixtures with phosphatidylglycerol. The detailed characterization of phospholipid-assisted refolding reported here further supports a specific rather than nonspecific role for PE in structural maturation of lactose permease in vivo (Bogdanov, RI., and Dowhan, W, (1998) EMBO J, 17, 5255-5264).
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收藏
页码:12339 / 12345
页数:7
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