| Protein-membrane interaction and fatty acid transfer from intestinal fatty acid-binding protein to membranes. Support for a multistep process. | |
| | |
MedLine Citation:
|
PMID: 16551626 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Fatty acid transfer from intestinal fatty acid-binding protein (IFABP) to phospholipid membranes occurs during protein-membrane collisions. Electrostatic interactions involving the alpha-helical "portal" region of the protein have been shown to be of great importance. In the present study, the role of specific lysine residues in the alpha-helical region of IFABP was directly examined. A series of point mutants in rat IFABP was engineered in which the lysine positive charges in this domain were eliminated or reversed. Using a fluorescence resonance energy transfer assay, we analyzed the rates and mechanism of fatty acid transfer from wild type and mutant proteins to acceptor membranes. Most of the alpha-helical domain mutants showed slower absolute fatty acid transfer rates to zwitterionic membranes, with substitution of one of the lysines of the alpha2 helix, Lys27, resulting in a particularly dramatic decrease in the fatty acid transfer rate. Sensitivity to negatively charged phospholipid membranes was also reduced, with charge reversal mutants in the alpha2 helix the most affected. The results support the hypothesis that the portal region undergoes a conformational change during protein-membrane interaction, which leads to release of the bound fatty acid to the membrane and that the alpha2 segment is of particular importance in the establishment of charge-charge interactions between IFABP and membranes. Cross-linking experiments with a phospholipid-photoactivable reagent underscored the importance of charge-charge interactions, showing that the physical interaction between wild-type intestinal fatty acid-binding protein and phospholipid membranes is enhanced by electrostatic interactions. Protein-membrane interactions were also found to be enhanced by the presence of ligand, suggesting different collisional complex structures for holo- and apo-IFABP. |
| | |
Authors:
|
Lisandro J Falomir-Lockhart; Lisandro Laborde; Peter C Kahn; Judith Storch; Betina Córsico |
Related Documents
:
|
11374956 - New methoxylated fatty acids from the caribbean sponge callyspongia fallax. 8465966 - 31p nmr examination of phosphorus metabolites in the aqueous, acidic, and organic extra... 7354136 - Amino acid modulation of renal phosphatidylcholine biosynthesis in the rat. 406916 - Self-regulation of membrane fluidity. the effect of saturated normal and methoxy fatty ... 3677416 - Bile acid metabolism in cirrhotic liver tissue--altered synthesis and impaired hepatic ... 20085226 - Phenolic acids in the flowers of althaea rosea var. nigra. |
Publication Detail:
|
Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2006-03-21 |
Journal Detail:
|
Title: The Journal of biological chemistry Volume: 281 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2006 May |
Date Detail:
|
Created Date: 2006-05-15 Completed Date: 2006-07-21 Revised Date: 2008-11-21 |
Medline Journal Info:
|
Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
|
Languages: eng Pagination: 13979-89 Citation Subset: IM |
Affiliation:
|
Instituto de Investigaciones Bioquímicas de La Plata, CONICET-UNLP, Facultad de Ciencias Médicas, Calles 60 y 120, 1900-La Plata, Argentina. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Cell Membrane / metabolism* Cross-Linking Reagents / pharmacology Fatty Acid-Binding Proteins / metabolism* Fatty Acids / metabolism* Fluorescence Resonance Energy Transfer Models, Molecular Mutation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Rats Static Electricity |
| Grant Support | |
ID/Acronym/Agency:
|
DK 38389/DK/NIDDK NIH HHS; TW01100-01/TW/FIC NIH HHS |
| Chemical | |
Reg. No./Substance:
|
0/Cross-Linking Reagents; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomp...
Next Document: YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins.