| Phospholipid flop induced by transmembrane peptides in model membranes is modulated by lipid composition. | |
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MedLine Citation:
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PMID: 12515559 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Since phospholipid synthesis is generally confined to one leaflet of a membrane, membrane growth requires phospholipid translocation (flip-flop). It is generally assumed that this process is protein-mediated; however, the mechanism of flip-flop remains elusive. Previously, we have demonstrated flop of 2-[6-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]caproyl] (C6NBD) phospholipids, induced by the presence of membrane-spanning peptides in vesicles composed of an Escherichia coli phospholipid extract, supporting the hypothesis that the presence of transmembrane stretches of proteins in the bilayer is sufficient to allow phospholipid flip-flop in the inner membrane of E. coli [Kol et al. (2001) Biochemistry 40, 10500]. Here, we investigated whether the specific phospholipid composition of E. coli is a prerequisite for transmembrane helix-induced flop of phospholipids. This was tested by determining the amount of C6NBD-phospholipid that was translocated from the inner leaflet to the outer leaflet of a model membrane in time, using a dithionite reduction assay. The transmembrane peptides GWWL(AL)8WWA (WALP23) and GKKL(AL)8KKA (KALP23) induced phospholipid flop in model membranes composed of various lipid mixtures. The rate of peptide-induced flop was found to decrease with increasing dioleoylphosphatidylethanolamine (DOPE) content of vesicles composed of DOPE and dioleoylphosphatidylcholine (DOPC), and the rate of KALP23-induced flop was shown to be stimulated by higher dioleoylphosphatidylglycerol (DOPG) content in model membranes composed of DOPG and DOPC. Furthermore, the incorporation of cholesterol had an inhibitory effect on peptide-induced flop. Finally, flop efficiency was strongly dependent on the phospholipid headgroup of the NBD-phospholipid analogue. Possible implications for transmembrane helix-induced flop in biomembranes in general are discussed. |
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Authors:
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Matthijs A Kol; Adrianus N C van Laak; Dirk T S Rijkers; J Antoinette Killian; Anton I P M de Kroon; Ben de Kruijff |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochemistry Volume: 42 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 2003 Jan |
Date Detail:
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Created Date: 2003-01-07 Completed Date: 2003-02-28 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 231-7 Citation Subset: IM |
Affiliation:
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Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. m.a.kol@chem.uu.nl |
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| MeSH Terms | |
Descriptor/Qualifier:
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4-Chloro-7-nitrobenzofurazan
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analogs & derivatives*,
chemistry Biological Transport Cholesterol / chemistry Escherichia coli / chemistry Kinetics Lipid Bilayers / chemistry* Lipids / analysis, chemistry* Lysine / chemistry Membrane Proteins / chemistry* Models, Biological Oxadiazoles / chemistry Peptides / chemistry* Phosphatidylcholines / chemistry Phosphatidylethanolamines / chemistry Phosphatidylglycerols / chemistry Phosphatidylserines / chemistry Phospholipids / chemistry* Protein Structure, Secondary Tryptophan / chemistry |
| Chemical | |
Reg. No./Substance:
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0/1-palmitoyl-2-(6-((7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)caproyl)glycero-3-phosphoserine; 0/C6NBD-phosphatidylglycerol; 0/Lipid Bilayers; 0/Lipids; 0/Membrane Proteins; 0/Oxadiazoles; 0/Peptides; 0/Phosphatidylcholines; 0/Phosphatidylethanolamines; 0/Phosphatidylglycerols; 0/Phosphatidylserines; 0/Phospholipids; 10015-85-7/1,2-oleoylphosphatidylcholine; 10199-89-0/4-Chloro-7-nitrobenzofurazan; 108762-10-3/1,2-(palmitoyl-NBD-aminocaproyl)phosphatidylethanolamine; 56-87-1/Lysine; 57-88-5/Cholesterol; 73-22-3/Tryptophan |
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