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Article: The Arabidopsis acbp1acbp2 double mutant lacking acyl-CoA-binding proteins ACBP1 and ACBP2 is embryo lethal

TitleThe Arabidopsis acbp1acbp2 double mutant lacking acyl-CoA-binding proteins ACBP1 and ACBP2 is embryo lethal
Authors
Issue Date2010
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPH
Citation
New Phytologist, 2010, v. 186 n. 4, p. 843-855 How to Cite?
Abstract•In Arabidopsis thaliana, the amino acid sequences of membrane-associated acyl-CoA-binding proteins ACBP1 and ACBP2 are highly conserved. We have shown previously that, in developing seeds, ACBP1 accumulates in the cotyledonary cells of embryos and ACBP1 is proposed to be involved in lipid transfer. We show here by immunolocalization, using ACBP2-specific antibodies, that ACBP2 is also expressed in the embryos at various stages of seed development in Arabidopsis.•Phenotypic analyses of acbp1 and acbp2 single mutants revealed that knockout of either ACBP1 or ACBP2 alone did not affect their life cycle as both single mutants exhibited normal growth and development similar to the wild-type. However, the acbp1acbp2 double mutant was embryo lethal and was also defective in callus induction.•On lipid and acyl-CoA analyses, the siliques, but not the leaves, of the acbp1 mutant accumulated galactolipid monogalactosyldiacylglycerol and 18:0-CoA, but the levels of most polyunsaturated species of phospholipid, such as phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine, declined.•As recombinant ACBP1 and ACBP2 bind unsaturated phosphatidylcholine and acyl-CoA esters in vitro, we propose that ACBP1 and ACBP2 are essential in lipid transfer during early embryogenesis in Arabidopsis. © The Authors (2010). Journal compilation © New Phytologist Trust (2010).
Persistent Identifierhttp://hdl.handle.net/10722/179194
ISSN
2015 Impact Factor: 7.21
2015 SCImago Journal Rankings: 3.603
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChen, Qen_US
dc.contributor.authorXiao, Sen_US
dc.contributor.authorQi, Wen_US
dc.contributor.authorMishra, Gen_US
dc.contributor.authorMa, Jen_US
dc.contributor.authorWang, Men_US
dc.contributor.authorChye, Men_US
dc.date.accessioned2012-12-19T09:52:46Z-
dc.date.available2012-12-19T09:52:46Z-
dc.date.issued2010en_US
dc.identifier.citationNew Phytologist, 2010, v. 186 n. 4, p. 843-855en_US
dc.identifier.issn0028-646Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/179194-
dc.description.abstract•In Arabidopsis thaliana, the amino acid sequences of membrane-associated acyl-CoA-binding proteins ACBP1 and ACBP2 are highly conserved. We have shown previously that, in developing seeds, ACBP1 accumulates in the cotyledonary cells of embryos and ACBP1 is proposed to be involved in lipid transfer. We show here by immunolocalization, using ACBP2-specific antibodies, that ACBP2 is also expressed in the embryos at various stages of seed development in Arabidopsis.•Phenotypic analyses of acbp1 and acbp2 single mutants revealed that knockout of either ACBP1 or ACBP2 alone did not affect their life cycle as both single mutants exhibited normal growth and development similar to the wild-type. However, the acbp1acbp2 double mutant was embryo lethal and was also defective in callus induction.•On lipid and acyl-CoA analyses, the siliques, but not the leaves, of the acbp1 mutant accumulated galactolipid monogalactosyldiacylglycerol and 18:0-CoA, but the levels of most polyunsaturated species of phospholipid, such as phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine, declined.•As recombinant ACBP1 and ACBP2 bind unsaturated phosphatidylcholine and acyl-CoA esters in vitro, we propose that ACBP1 and ACBP2 are essential in lipid transfer during early embryogenesis in Arabidopsis. © The Authors (2010). Journal compilation © New Phytologist Trust (2010).en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NPHen_US
dc.relation.ispartofNew Phytologisten_US
dc.rightsNew Phytologist. Copyright © Blackwell Publishing Ltd.-
dc.subject.meshAcyl Coenzyme A - Metabolismen_US
dc.subject.meshArabidopsis - Cytology - Embryology - Geneticsen_US
dc.subject.meshArabidopsis Proteins - Genetics - Metabolismen_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshGene Expression Regulation, Developmentalen_US
dc.subject.meshGene Expression Regulation, Planten_US
dc.subject.meshGene Knockout Techniquesen_US
dc.subject.meshGenotypeen_US
dc.subject.meshKanamycin Resistance - Geneticsen_US
dc.subject.meshLipid Metabolismen_US
dc.subject.meshMembrane Lipids - Metabolismen_US
dc.subject.meshMutation - Geneticsen_US
dc.subject.meshOligonucleotide Array Sequence Analysisen_US
dc.subject.meshPhosphatidylcholines - Metabolismen_US
dc.subject.meshPlant Leaves - Genetics - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshSeeds - Cytology - Geneticsen_US
dc.titleThe Arabidopsis acbp1acbp2 double mutant lacking acyl-CoA-binding proteins ACBP1 and ACBP2 is embryo lethalen_US
dc.typeArticleen_US
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_US
dc.identifier.emailWang, M: mfwang@hku.hken_US
dc.identifier.emailChye, M: mlchye@hkucc.hku.hken_US
dc.identifier.authorityXiao, S=rp00817en_US
dc.identifier.authorityWang, M=rp00800en_US
dc.identifier.authorityChye, M=rp00687en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1111/j.1469-8137.2010.03231.xen_US
dc.identifier.pmid20345632-
dc.identifier.pmcidPMC4169659-
dc.identifier.scopuseid_2-s2.0-77953521913en_US
dc.identifier.hkuros170233-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77953521913&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume186en_US
dc.identifier.issue4en_US
dc.identifier.spage843en_US
dc.identifier.epage855en_US
dc.identifier.eissn1469-8137-
dc.identifier.isiWOS:000277526900007-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridChen, Q=7406335399en_US
dc.identifier.scopusauthoridXiao, S=7402022635en_US
dc.identifier.scopusauthoridQi, W=55119073400en_US
dc.identifier.scopusauthoridMishra, G=12809587900en_US
dc.identifier.scopusauthoridMa, J=9248720900en_US
dc.identifier.scopusauthoridWang, M=7406691844en_US
dc.identifier.scopusauthoridChye, M=7003905460en_US
dc.identifier.citeulike7163333-

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