Document Detail


Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone.
MedLine Citation:
PMID:  10212204     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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-1-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, M., and Dowhan, W. (1998) EMBO J. 17, 5255-5264).
Authors:
M Bogdanov; M Umeda; W Dowhan
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  274     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1999 Apr 
Date Detail:
Created Date:  1999-06-03     Completed Date:  1999-06-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  12339-45     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, University of Texas-Houston Medical School, Houston, Texas 77225, USA.
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MeSH Terms
Descriptor/Qualifier:
Amines / chemistry
Escherichia coli Proteins*
Membrane Proteins / metabolism*
Membrane Transport Proteins / metabolism
Methylation
Molecular Chaperones / chemistry,  metabolism*
Monosaccharide Transport Proteins*
Phosphatidylethanolamines / chemistry,  metabolism*
Protein Folding
Symporters*
Grant Support
ID/Acronym/Agency:
GM24078/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Amines; 0/Escherichia coli Proteins; 0/LacY protein, E coli; 0/Membrane Proteins; 0/Membrane Transport Proteins; 0/Molecular Chaperones; 0/Monosaccharide Transport Proteins; 0/Phosphatidylethanolamines; 0/Symporters; 9068-45-5/lactose permease

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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