| Arabidopsis LONG-CHAIN ACYL-COA SYNTHETASE 1 (LACS1), LACS2, and LACS3 facilitate fatty acid uptake in yeast. | |
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MedLine Citation:
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PMID: 22153237 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The plant cuticle is a lipid-based barrier on the aerial surfaces of plants that plays a variety of protective roles. The cuticle is comprised largely of long-chain and very-long-chain fatty acids and their derivatives. In Arabidopsis, LONG-CHAIN ACYL-COA SYNTHETASE1 (LACS1), LACS2, and LACS3 are known or suspected cuticle biosynthetic genes. Very-long-chain acyl-coenzyme A (CoA) synthetase activity has been demonstrated for LACS1 and LACS2, although the role for such an activity in cuticle biosynthesis is currently unclear. In yeast and mammalian systems, some very-long-chain acyl-CoA synthetases are also called fatty acid transport proteins (FATPs) due to a second function of mediating transmembrane movement of fatty acids. We sought to determine if LACS1-3 also have this dual functionality. A yeast fat1Δ mutant is deficient in both very-long-chain acyl-CoA synthetase activity and exogenous fatty acid uptake. We demonstrate that heterologous expression of LACS1, 2, or 3 is able to complement both of these deficiencies. Furthermore, expression of each LACS enzyme in yeast resulted in uptake of the long-chain fatty acid analogue, C(1)-BODIPY-C(12). Only expression of LACS1 resulted in uptake of the very-long-chain fatty acid analogue, BODIPY-C(16). These results demonstrate that LACS1, LACS2, and LACS3 have the dual functionality of yeast and mammalian FATP enzymes. These findings have implications in the transmembrane transport and intracellular trafficking of plant lipids destined for export to the cuticle. |
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Authors:
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Ian P Pulsifer; Sabine Kluge; Owen Rowland |
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Publication Detail:
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Type: Journal Article Date: 2011-10-18 |
Journal Detail:
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Title: Plant physiology and biochemistry : PPB / Société française de physiologie végétale Volume: 51 ISSN: 1873-2690 ISO Abbreviation: Plant Physiol. Biochem. Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2011-12-14 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9882449 Medline TA: Plant Physiol Biochem Country: France |
Other Details:
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Languages: eng Pagination: 31-9 Citation Subset: IM |
Copyright Information:
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Copyright © 2011 Elsevier Masson SAS. All rights reserved. |
Affiliation:
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Department of Biology and Institute of Biochemistry, Carleton University, 1125 Colonel By Drive, Ottawa, Ontario K1S 5B6, Canada. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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