Document Detail


Diverse effects of phospholipids on lipoprotein sorting and ATP hydrolysis by the ABC transporter LolCDE complex.
MedLine Citation:
PMID:  17498646     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The LolCDE complex of Escherichia coli releases outer membrane-specific lipoproteins from the inner membrane. Lipoproteins with Asp at +2 remain in the inner membrane since this residue functions as a LolCDE avoidance signal depending on phosphatidylethanolamine. We examined the effects of other phospholipids on lipoprotein sorting in proteoliposomes reconstituted with LolCDE and various synthetic phospholipids. The lipoprotein release and ATP hydrolysis were both low at 2 mM Mg(2+) but very high at 10 mM Mg(2+) in proteoliposomes containing cardiolipin alone. However, the Lol avoidance function was abolished at 10 mM Mg(2+), and the release of lipoproteins with Asp at +2 was as efficient as that of outer membrane-specific lipoproteins. The addition of phosphatidylethanolamine to cardiolipin stimulated the ATP hydrolysis and increased the Lol avoidance function of Asp at +2 at 2 mM Mg(2+). The addition of phosphatidylglycerol to cardiolipin nearly completely inhibited the release of lipoproteins with Asp at +2 even at 10 mM Mg(2+), while that of outer membrane-specific lipoproteins was not. Taken together, these results indicate that three major phospholipids of E. coli differently affect lipoprotein sorting and the activity of LolCDE.
Authors:
Shigehiko Miyamoto; Hajime Tokuda
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-04-14
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1768     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2007 Jul 
Date Detail:
Created Date:  2007-06-15     Completed Date:  2007-08-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1848-54     Citation Subset:  IM    
Affiliation:
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Tokyo 113-0032, Japan.
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MeSH Terms
Descriptor/Qualifier:
ATP-Binding Cassette Transporters / metabolism*
Adenosine Triphosphate / metabolism*
Bacterial Outer Membrane Proteins / metabolism
Cardiolipins / metabolism,  pharmacology
Carrier Proteins / metabolism
Escherichia coli Proteins / metabolism*
Lipoproteins / drug effects,  metabolism*
Liposomes / metabolism
Magnesium / physiology
Periplasmic Binding Proteins / metabolism
Phosphatidylethanolamines / pharmacology
Phosphatidylglycerols / pharmacology
Phospholipids / pharmacology*
Protein Transport / drug effects*
Proteolipids / drug effects,  metabolism
Chemical
Reg. No./Substance:
0/ATP-Binding Cassette Transporters; 0/Bacterial Outer Membrane Proteins; 0/Cardiolipins; 0/Carrier Proteins; 0/Escherichia coli Proteins; 0/Lipoproteins; 0/Liposomes; 0/LolA protein, E coli; 0/LolB protein, E coli; 0/LolC protein, E coli; 0/LolD protein, E coli; 0/LolE protein, E coli; 0/Periplasmic Binding Proteins; 0/Phosphatidylethanolamines; 0/Phosphatidylglycerols; 0/Phospholipids; 0/Proteolipids; 0/proteoliposomes; 39382-08-6/phosphatidylethanolamine; 56-65-5/Adenosine Triphosphate; 7439-95-4/Magnesium

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


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