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Article: Arabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-metal-binding farnesylated protein AtFP6

TitleArabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-metal-binding farnesylated protein AtFP6
Authors
KeywordsArabidopsis thaliana acyl-CoA-binding protein (ACBP)
AtFP6
Farnesylated protein
Heavy metals
Metal-binding motif
Plasma membrane
Protein-protein interaction
Issue Date2009
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
Citation
New Phytologist, 2009, v. 181 n. 1, p. 89-102 How to Cite?
Abstract• Arabidopsis thaliana acyl-CoA-binding protein 2 (ACBP2) was observed to interact with farnesylated protein 6 (AtFP6), which has a metal-binding motif (M/LXCXXC). Their interaction and expression in response to heavy metals were investigated. • Yeast two-hybrid analysis and in vitro assays showed that an ACBP2 derivative lacking ankyrin repeats did not interact with AtFP6, indicating that the ankyrin repeats mediate protein-protein interaction. Autofluorescence-tagged ACBP2 and AtFP6 transiently co-expressed in tobacco (Nicotiana tabacum) were both targeted to the plasma membrane. • Reverse transcriptase polymerase chain reaction and northern blot analyses revealed that AtFP6 mRNA was induced by cadmium (Cd(II)) in A. thaliana roots. Assays using metal-chelate affinity chromatography demonstrated that in vitro translated ACBP2 and AtFP6 bound lead (Pb(II)), Cd(II) and copper (Cu(II)). Consistently, assays using fluorescence analysis confirmed that (His) 6-AtFP6 bound Pb(II), like (His) 6-ACBP2. • Arabidopsis thaliana plants overexpressing ACBP2 or AtFP6 were more tolerant to Cd(II) than wild-type plants. Plasma membrane-localized ACBP2 and AtFP6 probably mediate Pb(II), Cd(II) and Cu(II) transport in A. thaliana roots. Also, (His) 6-ACBP2 binds [ 14C]linoleoyl-CoA and [ 14C]linolenoyl-CoA, the precursors for phospholipid repair following lipid peroxidation under heavy metal stress at the plasma membrane. ACBP2-overexpressing plants were more tolerant to hydrogen peroxide than wild-type plants, further supporting a role for ACBP2 in post-stress membrane repair. © The Authors (2008).
Persistent Identifierhttp://hdl.handle.net/10722/149707
ISSN
2015 Impact Factor: 7.21
2015 SCImago Journal Rankings: 3.603
ISI Accession Number ID
Funding AgencyGrant Number
University Grants Committee of the Hong Kong Special Administrative Region, ChinaAoE/B-07/99
University of Hong Kong10208034
Croucher Senior Research Fellowship
University of Hong Kong and HL
Funding Information:

We thank M. M. Goodin (University of California, Berkeley) for vectors pGDR and pGDG, M. Frentzen (Institut fur Biologie I, Aachen) for BnLPAAT cDNA and W. K. Yip for provision of the Biolistic PDS- 1000/He system. This work was supported by the University Grants Committee of the Hong Kong Special Administrative Region, China (Project No. AoE/B-07/99), the University of Hong Kong (10208034) and a Croucher Senior Research Fellowship awarded to MLC. WG and SX were supported by postgraduate studentships from the University of Hong Kong and HL by the Croucher Foundation.

References

 

DC FieldValueLanguage
dc.contributor.authorGao, Wen_HK
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorLi, HYen_HK
dc.contributor.authorTsao, SWen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2012-06-26T05:57:24Z-
dc.date.available2012-06-26T05:57:24Z-
dc.date.issued2009en_HK
dc.identifier.citationNew Phytologist, 2009, v. 181 n. 1, p. 89-102en_HK
dc.identifier.issn0028-646Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/149707-
dc.description.abstract• Arabidopsis thaliana acyl-CoA-binding protein 2 (ACBP2) was observed to interact with farnesylated protein 6 (AtFP6), which has a metal-binding motif (M/LXCXXC). Their interaction and expression in response to heavy metals were investigated. • Yeast two-hybrid analysis and in vitro assays showed that an ACBP2 derivative lacking ankyrin repeats did not interact with AtFP6, indicating that the ankyrin repeats mediate protein-protein interaction. Autofluorescence-tagged ACBP2 and AtFP6 transiently co-expressed in tobacco (Nicotiana tabacum) were both targeted to the plasma membrane. • Reverse transcriptase polymerase chain reaction and northern blot analyses revealed that AtFP6 mRNA was induced by cadmium (Cd(II)) in A. thaliana roots. Assays using metal-chelate affinity chromatography demonstrated that in vitro translated ACBP2 and AtFP6 bound lead (Pb(II)), Cd(II) and copper (Cu(II)). Consistently, assays using fluorescence analysis confirmed that (His) 6-AtFP6 bound Pb(II), like (His) 6-ACBP2. • Arabidopsis thaliana plants overexpressing ACBP2 or AtFP6 were more tolerant to Cd(II) than wild-type plants. Plasma membrane-localized ACBP2 and AtFP6 probably mediate Pb(II), Cd(II) and Cu(II) transport in A. thaliana roots. Also, (His) 6-ACBP2 binds [ 14C]linoleoyl-CoA and [ 14C]linolenoyl-CoA, the precursors for phospholipid repair following lipid peroxidation under heavy metal stress at the plasma membrane. ACBP2-overexpressing plants were more tolerant to hydrogen peroxide than wild-type plants, further supporting a role for ACBP2 in post-stress membrane repair. © The Authors (2008).en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPHen_HK
dc.relation.ispartofNew Phytologisten_HK
dc.subjectArabidopsis thaliana acyl-CoA-binding protein (ACBP)en_HK
dc.subjectAtFP6en_HK
dc.subjectFarnesylated proteinen_HK
dc.subjectHeavy metalsen_HK
dc.subjectMetal-binding motifen_HK
dc.subjectPlasma membraneen_HK
dc.subjectProtein-protein interactionen_HK
dc.subject.meshAnkyrin Repeat - Physiologyen_US
dc.subject.meshArabidopsis - Metabolismen_US
dc.subject.meshArabidopsis Proteins - Metabolismen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCell Membrane - Metabolismen_US
dc.subject.meshHydrogen Peroxideen_US
dc.subject.meshLipid Peroxidationen_US
dc.subject.meshMetals, Heavy - Metabolismen_US
dc.subject.meshProtein Prenylationen_US
dc.subject.meshRna, Messenger - Biosynthesisen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.titleArabidopsis thaliana acyl-CoA-binding protein ACBP2 interacts with heavy-metal-binding farnesylated protein AtFP6en_HK
dc.typeArticleen_HK
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_HK
dc.identifier.emailTsao, SW: gswtsao@hku.hken_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityXiao, S=rp00817en_HK
dc.identifier.authorityTsao, SW=rp00399en_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1111/j.1469-8137.2008.02631.xen_HK
dc.identifier.pmid18823312-
dc.identifier.scopuseid_2-s2.0-57449094676en_HK
dc.identifier.hkuros154147-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-57449094676&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume181en_HK
dc.identifier.issue1en_HK
dc.identifier.spage89en_HK
dc.identifier.epage102en_HK
dc.identifier.isiWOS:000261397400011-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridGao, W=36045713300en_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridLi, HY=22953303900en_HK
dc.identifier.scopusauthoridTsao, SW=7102813116en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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