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Article: Membrane localization of Arabidopsis acyl-CoA binding protein ACBP2

TitleMembrane localization of Arabidopsis acyl-CoA binding protein ACBP2
Authors
Keywordsacyl-CoA transfer
Green fluorescencent protein
Lipid metabolism
Protein targeting
Subcellular fractionation
Transmembrane domain
Issue Date2003
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, 2003, v. 51 n. 4, p. 483-492 How to Cite?
AbstractCytosolic acyl-CoA binding proteins bind long-chain acyl-CoAs and act as intracellular acyl-CoA transporters and pool formers. Recently, we have characterized Arabidopsis thaliana cDNAs encoding novel forms of ACBP, designated ACBP1 and ACBP2, that contain a hydrophobic domain at the N-terminus and show conservation at the acyl-CoA binding domain to cytosolic ACBPs. We have previously demonstrated that ACBP1 is membrane-associated in Arabidopsis. Here, western blot analysis of anti-ACBP2 antibodies on A. thaliana protein showed that ACBP2 is located in the microsome-containing membrane fraction and in the subcellular fraction containing large particles (mitochondria, chloroplasts and peroxisomes), resembling the subcellular localization of ACBP1. To further investigate the subcellular localization of ACBP2, we fused ACBP2 translationally in-frame to GFP. By means of particle gene bombardment, ACBP2-GFP and ACBP1-GFP fusion proteins were observed transiently expressed at the plasma membrane and at the endoplasmic reticulum in onion epidermal cells. GFP fusions with deletion derivatives of ACBP1 or ACBP2 lacking the transmembrane domain were impaired in membrane targeting. Our investigations also showed that when the transmembrane domain of ACBP1 or that of ACBP2 was fused with GFP, the fusion protein was targeted to the plasma membrane, thereby establishing their role in membrane targeting. The localization of ACBP1-GFP is consistent with our previous observations using immunoelectron microscopy whereby ACBP1 was localized to the plasma membrane and vesicles. We conclude that ACBP2, like ACBP1, is a membrane protein that likely functions in membrane-associated acyl-CoA transfer/metabolism.
Persistent Identifierhttp://hdl.handle.net/10722/68665
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 1.915
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, HYen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-09-06T06:06:35Z-
dc.date.available2010-09-06T06:06:35Z-
dc.date.issued2003en_HK
dc.identifier.citationPlant Molecular Biology, 2003, v. 51 n. 4, p. 483-492en_HK
dc.identifier.issn0167-4412en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68665-
dc.description.abstractCytosolic acyl-CoA binding proteins bind long-chain acyl-CoAs and act as intracellular acyl-CoA transporters and pool formers. Recently, we have characterized Arabidopsis thaliana cDNAs encoding novel forms of ACBP, designated ACBP1 and ACBP2, that contain a hydrophobic domain at the N-terminus and show conservation at the acyl-CoA binding domain to cytosolic ACBPs. We have previously demonstrated that ACBP1 is membrane-associated in Arabidopsis. Here, western blot analysis of anti-ACBP2 antibodies on A. thaliana protein showed that ACBP2 is located in the microsome-containing membrane fraction and in the subcellular fraction containing large particles (mitochondria, chloroplasts and peroxisomes), resembling the subcellular localization of ACBP1. To further investigate the subcellular localization of ACBP2, we fused ACBP2 translationally in-frame to GFP. By means of particle gene bombardment, ACBP2-GFP and ACBP1-GFP fusion proteins were observed transiently expressed at the plasma membrane and at the endoplasmic reticulum in onion epidermal cells. GFP fusions with deletion derivatives of ACBP1 or ACBP2 lacking the transmembrane domain were impaired in membrane targeting. Our investigations also showed that when the transmembrane domain of ACBP1 or that of ACBP2 was fused with GFP, the fusion protein was targeted to the plasma membrane, thereby establishing their role in membrane targeting. The localization of ACBP1-GFP is consistent with our previous observations using immunoelectron microscopy whereby ACBP1 was localized to the plasma membrane and vesicles. We conclude that ACBP2, like ACBP1, is a membrane protein that likely functions in membrane-associated acyl-CoA transfer/metabolism.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412en_HK
dc.relation.ispartofPlant Molecular Biologyen_HK
dc.subjectacyl-CoA transferen_HK
dc.subjectGreen fluorescencent proteinen_HK
dc.subjectLipid metabolismen_HK
dc.subjectProtein targetingen_HK
dc.subjectSubcellular fractionationen_HK
dc.subjectTransmembrane domainen_HK
dc.titleMembrane localization of Arabidopsis acyl-CoA binding protein ACBP2en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0167-4412&volume=51&spage=483&epage=492&date=2003&atitle=Membrane+localization+of+Arabidopsis+acyl-CoA+binding+protein+ACBP2en_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1023/A:1022330304402en_HK
dc.identifier.pmid12650615-
dc.identifier.scopuseid_2-s2.0-0037342067en_HK
dc.identifier.hkuros75788en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037342067&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume51en_HK
dc.identifier.issue4en_HK
dc.identifier.spage483en_HK
dc.identifier.epage492en_HK
dc.identifier.isiWOS:000181012500004-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridLi, HY=22953303900en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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