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Article: Arabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly localized to the cytosol and ACBP4 depletion affects membrane lipid composition

TitleArabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly localized to the cytosol and ACBP4 depletion affects membrane lipid composition
Authors
Issue Date2008
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412
Citation
Plant Molecular Biology, 2008, v. 68 n. 6, p. 571-583 How to Cite?
AbstractIn Arabidopsis thaliana, acyl-CoA-binding proteins (ACBPs) are encoded by six genes, and they display varying affinities for acyl-CoA esters. Recombinant ACBP4 and ACBP5 have been shown to bind oleoyl-CoA esters in vitro. In this study, the subcellular localizations of ACBP4 and ACBP5 were determined by biochemical fractionation followed by western blot analyses using anti-ACBP4 and anti-ACBP5 antibodies and immuno-electron microscopy. Confocal microscopy of autofluorescence-tagged ACBP4 and ACBP5, expressed transiently in onion epidermal cells and in transgenic Arabidopsis, confirmed their expression in the cytosol. Taken together, ACBP4 and ACBP5 are available in the cytosol to bind and transfer cytosolic oleoyl-CoA esters. Lipid profile analysis further revealed that an acbp4 knockout mutant showed decreases in membrane lipids (digalactosyldiacylglycerol, monogalactosyldiacylglycerol, phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol) while acbp4-complemented lines attained levels similar to wild type, suggesting that ACBP4 plays a role in the biosynthesis of membrane lipids including galactolipids and phospholipids. © 2008 Springer Science+Business Media B.V.
Persistent Identifierhttp://hdl.handle.net/10722/179094
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 1.915
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXiao, Sen_US
dc.contributor.authorLi, HYen_US
dc.contributor.authorZhang, JPen_US
dc.contributor.authorChan, SWen_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2012-12-19T09:51:56Z-
dc.date.available2012-12-19T09:51:56Z-
dc.date.issued2008en_US
dc.identifier.citationPlant Molecular Biology, 2008, v. 68 n. 6, p. 571-583en_US
dc.identifier.issn0167-4412en_US
dc.identifier.urihttp://hdl.handle.net/10722/179094-
dc.description.abstractIn Arabidopsis thaliana, acyl-CoA-binding proteins (ACBPs) are encoded by six genes, and they display varying affinities for acyl-CoA esters. Recombinant ACBP4 and ACBP5 have been shown to bind oleoyl-CoA esters in vitro. In this study, the subcellular localizations of ACBP4 and ACBP5 were determined by biochemical fractionation followed by western blot analyses using anti-ACBP4 and anti-ACBP5 antibodies and immuno-electron microscopy. Confocal microscopy of autofluorescence-tagged ACBP4 and ACBP5, expressed transiently in onion epidermal cells and in transgenic Arabidopsis, confirmed their expression in the cytosol. Taken together, ACBP4 and ACBP5 are available in the cytosol to bind and transfer cytosolic oleoyl-CoA esters. Lipid profile analysis further revealed that an acbp4 knockout mutant showed decreases in membrane lipids (digalactosyldiacylglycerol, monogalactosyldiacylglycerol, phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol) while acbp4-complemented lines attained levels similar to wild type, suggesting that ACBP4 plays a role in the biosynthesis of membrane lipids including galactolipids and phospholipids. © 2008 Springer Science+Business Media B.V.en_US
dc.languageengen_US
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412en_US
dc.relation.ispartofPlant Molecular Biologyen_US
dc.subject.meshArabidopsis - Metabolismen_US
dc.subject.meshArabidopsis Proteins - Metabolismen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshDna Primersen_US
dc.subject.meshGene Knockout Techniquesen_US
dc.subject.meshMembrane Lipids - Metabolismen_US
dc.subject.meshMicroscopy, Confocalen_US
dc.subject.meshMicroscopy, Fluorescenceen_US
dc.subject.meshPlants, Genetically Modifieden_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshSubcellular Fractions - Metabolismen_US
dc.titleArabidopsis acyl-CoA-binding proteins ACBP4 and ACBP5 are subcellularly localized to the cytosol and ACBP4 depletion affects membrane lipid compositionen_US
dc.typeArticleen_US
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_US
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_US
dc.identifier.authorityXiao, S=rp00817en_US
dc.identifier.authorityChye, ML=rp00687en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s11103-008-9392-7en_US
dc.identifier.pmid18773301-
dc.identifier.scopuseid_2-s2.0-54849435430en_US
dc.identifier.hkuros154144-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-54849435430&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume68en_US
dc.identifier.issue6en_US
dc.identifier.spage571en_US
dc.identifier.epage583en_US
dc.identifier.isiWOS:000260378600004-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridXiao, S=7402022635en_US
dc.identifier.scopusauthoridLi, HY=22953303900en_US
dc.identifier.scopusauthoridZhang, JP=24759458400en_US
dc.identifier.scopusauthoridChan, SW=24758152300en_US
dc.identifier.scopusauthoridChye, ML=7003905460en_US

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