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Article: Light-regulated Arabidopsis ACBP4 and ACBP5 encode cytosolic acyl-CoA-binding proteins that bind phosphatidylcholine and oleoyl-CoA ester

TitleLight-regulated Arabidopsis ACBP4 and ACBP5 encode cytosolic acyl-CoA-binding proteins that bind phosphatidylcholine and oleoyl-CoA ester
Authors
KeywordsAcyl-CoA-binding protein
Light-regulation
Lipid metabolism
Lipid transfer
Oleoyl-CoA
Issue Date2009
PublisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/plaphy
Citation
Plant Physiology And Biochemistry, 2009, v. 47 n. 10, p. 926-933 How to Cite?
AbstractIn Arabidopsis thaliana, six genes encode acyl-CoA-binding proteins (ACBPs) that show conservation of an acyl-CoA-binding domain. These ACBPs display varying affinities for acyl-CoA esters, suggesting of different cellular roles. We have recently reported that three members (ACBP4, ACBP5 and ACBP6) are subcellularly localized to the cytosol by biochemical fractionation, confocal microscopy of transgenic Arabidopsis expressing autofluorescence-tagged fusions and immuno-electron microscopy using ACBP-specific antibodies. In this study, we observed by Northern blot analysis that ACBP4 and ACBP5 mRNAs in rosettes were up-regulated by light and dampened-off in darkness, mimicking FAD7 which encodes omega-3-fatty acid desaturase, an enzyme involved in plastidial lipid metabolism. Results from in vitro binding assays indicate that recombinant ACBP4 and ACBP5 proteins bind [14C]oleoyl-CoA esters better than recombinant ACBP6, suggesting that light-regulated ACBP4 and ACBP5 encode cytosolic ACBPs that are potential candidates for the intracellular transport of oleoyl-CoA ester exported from the chloroplast to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids. Nonetheless, His-tagged ACBP4 and ACBP5 resemble ACBP6 in their ability to bind phosphatidylcholine suggesting that all three ACBPs are available for the intracellular transfer of phosphatidylcholine. © 2009 Elsevier Masson SAS. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/89210
ISSN
2015 Impact Factor: 2.928
2015 SCImago Journal Rankings: 1.167
ISI Accession Number ID
Funding AgencyGrant Number
Croucher Senior Research Fellowship
University of Hong Kong10208034
10208270
University Grants Committee of the Hong Kong Special Administrative Region, ChinaAoE/B-07/99
Funding Information:

This work was supported by a Croucher Senior Research Fellowship (awarded to MLC) and the University of Hong Kong (10208034 and 10208270). SX was supported by a postdoctoral fellowship from the University of Hong Kong and the University Grants Committee of the Hong Kong Special Administrative Region, China (Project No. AoE/B-07/99). QFC was supported by a postgraduate studentship from the University of Hong Kong.

References

 

DC FieldValueLanguage
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorChen, QFen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-09-06T09:53:56Z-
dc.date.available2010-09-06T09:53:56Z-
dc.date.issued2009en_HK
dc.identifier.citationPlant Physiology And Biochemistry, 2009, v. 47 n. 10, p. 926-933en_HK
dc.identifier.issn0981-9428en_HK
dc.identifier.urihttp://hdl.handle.net/10722/89210-
dc.description.abstractIn Arabidopsis thaliana, six genes encode acyl-CoA-binding proteins (ACBPs) that show conservation of an acyl-CoA-binding domain. These ACBPs display varying affinities for acyl-CoA esters, suggesting of different cellular roles. We have recently reported that three members (ACBP4, ACBP5 and ACBP6) are subcellularly localized to the cytosol by biochemical fractionation, confocal microscopy of transgenic Arabidopsis expressing autofluorescence-tagged fusions and immuno-electron microscopy using ACBP-specific antibodies. In this study, we observed by Northern blot analysis that ACBP4 and ACBP5 mRNAs in rosettes were up-regulated by light and dampened-off in darkness, mimicking FAD7 which encodes omega-3-fatty acid desaturase, an enzyme involved in plastidial lipid metabolism. Results from in vitro binding assays indicate that recombinant ACBP4 and ACBP5 proteins bind [14C]oleoyl-CoA esters better than recombinant ACBP6, suggesting that light-regulated ACBP4 and ACBP5 encode cytosolic ACBPs that are potential candidates for the intracellular transport of oleoyl-CoA ester exported from the chloroplast to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids. Nonetheless, His-tagged ACBP4 and ACBP5 resemble ACBP6 in their ability to bind phosphatidylcholine suggesting that all three ACBPs are available for the intracellular transfer of phosphatidylcholine. © 2009 Elsevier Masson SAS. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/plaphyen_HK
dc.relation.ispartofPlant Physiology and Biochemistryen_HK
dc.rightsPlant Physiology and Biochemistry. Copyright © Elsevier France, Editions Scientifiques et Medicales.en_HK
dc.subjectAcyl-CoA-binding proteinen_HK
dc.subjectLight-regulationen_HK
dc.subjectLipid metabolismen_HK
dc.subjectLipid transferen_HK
dc.subjectOleoyl-CoAen_HK
dc.titleLight-regulated Arabidopsis ACBP4 and ACBP5 encode cytosolic acyl-CoA-binding proteins that bind phosphatidylcholine and oleoyl-CoA esteren_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0981-9428&volume=47&spage=926&epage=933&date=2009&atitle=Light-regulated+Arabidopsis+ACBP4+and+ACBP5+encode+cytosolic+acyl-CoA-binding+proteins+that+bind+phosphatidylcholine+and+oleoyl-CoA+esteren_HK
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityXiao, S=rp00817en_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.plaphy.2009.06.007en_HK
dc.identifier.pmid19589686-
dc.identifier.scopuseid_2-s2.0-68149165777en_HK
dc.identifier.hkuros165798en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-68149165777&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume47en_HK
dc.identifier.issue10en_HK
dc.identifier.spage926en_HK
dc.identifier.epage933en_HK
dc.identifier.isiWOS:000269586400009-
dc.publisher.placeFranceen_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridChen, QF=7406335399en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK
dc.identifier.citeulike5466104-

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