| Fatty acid transfer from Yarrowia lipolytica sterol carrier protein 2 to phospholipid membranes. | |
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MedLine Citation:
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PMID: 19580762 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sterol carrier protein 2 (SCP2) is an intracellular protein domain found in all forms of life. It was originally identified as a sterol transfer protein, but was recently shown to also bind phospholipids, fatty acids, and fatty-acyl-CoA with high affinity. Based on studies carried out in higher eukaryotes, it is believed that SCP2 targets its ligands to compartmentalized intracellular pools and participates in lipid traffic, signaling, and metabolism. However, the biological functions of SCP2 are incompletely characterized and may be different in microorganisms. Herein, we demonstrate the preferential localization of SCP2 of Yarrowia lipolytica (YLSCP2) in peroxisome-enriched fractions and examine the rate and mechanism of transfer of anthroyloxy fatty acid from YLSCP2 to a variety of phospholipid membranes using a fluorescence resonance energy transfer assay. The results show that fatty acids are transferred by a collision-mediated mechanism, and that negative charges on the membrane surface are important for establishing a "collisional complex". Phospholipids, which are major constituents of peroxisome and mitochondria, induce special effects on the rates of transfer. In conclusion, YLSCP2 may function as a fatty acid transporter with some degree of specificity, and probably diverts fatty acids to the peroxisomal metabolism. |
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Authors:
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Lisandro J Falomir Lockhart; Noelia I Burgardt; Raúl G Ferreyra; Marcelo Ceolin; Mario R Ermácora; Betina Córsico |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biophysical journal Volume: 97 ISSN: 1542-0086 ISO Abbreviation: Biophys. J. Publication Date: 2009 Jul |
Date Detail:
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Created Date: 2009-07-07 Completed Date: 2009-10-13 Revised Date: 2010-09-27 |
Medline Journal Info:
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Nlm Unique ID: 0370626 Medline TA: Biophys J Country: United States |
Other Details:
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Languages: eng Pagination: 248-56 Citation Subset: IM |
Affiliation:
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Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Facultad de Ciencias Médicas, Universidad Nacional de La Plata (UNLP), La Plata, Argentina. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Carrier Proteins
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chemistry,
genetics,
metabolism* Circular Dichroism Enzyme-Linked Immunosorbent Assay Escherichia coli Fatty Acids / metabolism* Fluorescence Resonance Energy Transfer Phospholipids / metabolism* Protein Binding Protein Structure, Secondary Recombinant Proteins / metabolism Sodium Chloride / metabolism Temperature Thermodynamics Unilamellar Liposomes / metabolism* Water / metabolism Yarrowia |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/Fatty Acids; 0/Phospholipids; 0/Recombinant Proteins; 0/Unilamellar Liposomes; 0/sterol carrier proteins; 7647-14-5/Sodium Chloride; 7732-18-5/Water |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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