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Article: Arabidopsis cytosolic acyl-CoA-binding proteins ACBP4, ACBP5 and ACBP6 have overlapping but distinct roles in seed development

TitleArabidopsis cytosolic acyl-CoA-binding proteins ACBP4, ACBP5 and ACBP6 have overlapping but distinct roles in seed development
Authors
Issue Date2014
PublisherPortland Press Ltd. The Journal's web site is located at http://www.bioscirep.org/
Citation
Bioscience Reports: molecular and cellular biology of the cell surface, 2014, v. 34 n. 6, p. 865-877, article no. e00165 How to Cite?
AbstractEukaryotic cytosolic ACBPs (acyl-CoA-binding proteins) bind acyl-CoA esters and maintain a cytosolic acyl-CoA pool, but the thermodynamics of their protein-lipid interactions and physiological relevance in plants are not well understood. Arabidopsis has three cytosolic ACBPs which have been identified as AtACBP4, AtACBP5 and AtACBP6, and microarray data indicated that all of them are expressed in seeds; AtACBP4 is expressed in early embryogenesis, whereas AtACBP5 is expressed later. ITC (isothermal titration calorimetry) in combination with transgenic Arabidopsis lines were used to investigate the roles of these three ACBPs from Arabidopsis thaliana. The dissociation constants, stoichiometry and enthalpy change of AtACBP interactions with various acyl-CoA esters were determined using ITC. Strong binding of recombinant (r) AtACBP6 with long-chain acyl-CoA (C16- to C18-CoA) esters was observed with dissociation constants in the nanomolar range. However, the affinity of rAtACBP4 and rAtACBP5 to these acyl-CoA esters was much weaker (dissociation constants in the micromolar range), suggesting that they interact with acyl-CoA esters differently from rAtACBP6. When transgenic Arabidopsis expressing AtACBP6pro::GUS was generated, strong GUS (β-glucuronidase) expression in cotyledonary-staged embryos and seedlings prompted us to measure the acyl-CoA contents of the acbp6 mutant. This mutant accumulated higher levels of C18:1-CoA and C18:1- and C18:2-CoAs in cotyledonary-staged embryos and seedlings, respectively, in comparison with the wild type. The acbp4acbp5acbp6 mutant showed the lightest seed weight and highest sensitivity to abscisic acid during germination, suggesting their physiological functions in seeds.
Persistent Identifierhttp://hdl.handle.net/10722/209287
ISSN
2015 Impact Factor: 2.446
2015 SCImago Journal Rankings: 1.123
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorHsiao, ASen_US
dc.contributor.authorHaslam, RPen_US
dc.contributor.authorMichaelson, LVen_US
dc.contributor.authorLiao, Pen_US
dc.contributor.authorChen, QFen_US
dc.contributor.authorSooriyaarachchi, Sen_US
dc.contributor.authorMowbray, SLen_US
dc.contributor.authorNapier, JAen_US
dc.contributor.authorTanner, JAen_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2015-04-17T05:03:54Z-
dc.date.available2015-04-17T05:03:54Z-
dc.date.issued2014en_US
dc.identifier.citationBioscience Reports: molecular and cellular biology of the cell surface, 2014, v. 34 n. 6, p. 865-877, article no. e00165en_US
dc.identifier.issn0144-8463en_US
dc.identifier.urihttp://hdl.handle.net/10722/209287-
dc.description.abstractEukaryotic cytosolic ACBPs (acyl-CoA-binding proteins) bind acyl-CoA esters and maintain a cytosolic acyl-CoA pool, but the thermodynamics of their protein-lipid interactions and physiological relevance in plants are not well understood. Arabidopsis has three cytosolic ACBPs which have been identified as AtACBP4, AtACBP5 and AtACBP6, and microarray data indicated that all of them are expressed in seeds; AtACBP4 is expressed in early embryogenesis, whereas AtACBP5 is expressed later. ITC (isothermal titration calorimetry) in combination with transgenic Arabidopsis lines were used to investigate the roles of these three ACBPs from Arabidopsis thaliana. The dissociation constants, stoichiometry and enthalpy change of AtACBP interactions with various acyl-CoA esters were determined using ITC. Strong binding of recombinant (r) AtACBP6 with long-chain acyl-CoA (C16- to C18-CoA) esters was observed with dissociation constants in the nanomolar range. However, the affinity of rAtACBP4 and rAtACBP5 to these acyl-CoA esters was much weaker (dissociation constants in the micromolar range), suggesting that they interact with acyl-CoA esters differently from rAtACBP6. When transgenic Arabidopsis expressing AtACBP6pro::GUS was generated, strong GUS (β-glucuronidase) expression in cotyledonary-staged embryos and seedlings prompted us to measure the acyl-CoA contents of the acbp6 mutant. This mutant accumulated higher levels of C18:1-CoA and C18:1- and C18:2-CoAs in cotyledonary-staged embryos and seedlings, respectively, in comparison with the wild type. The acbp4acbp5acbp6 mutant showed the lightest seed weight and highest sensitivity to abscisic acid during germination, suggesting their physiological functions in seeds.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.bioscirep.org/en_US
dc.relation.ispartofBioscience Reports: molecular and cellular biology of the cell surfaceen_US
dc.rightsThe final version of record is available at [Journal URL].en_US
dc.titleArabidopsis cytosolic acyl-CoA-binding proteins ACBP4, ACBP5 and ACBP6 have overlapping but distinct roles in seed developmenten_US
dc.typeArticleen_US
dc.identifier.emailChen, QF: chen2010@hku.hken_US
dc.identifier.emailTanner, JA: jatanner@hku.hken_US
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.identifier.authorityChye, ML=rp00687en_US
dc.identifier.doi10.1042/BSR20140139en_US
dc.identifier.pmid25423293en_US
dc.identifier.pmcidPMC4274664en_US
dc.identifier.hkuros242753en_US
dc.identifier.volume34en_US
dc.identifier.issue6en_US
dc.identifier.spage865en_US
dc.identifier.epage877, article no. e00165en_US
dc.publisher.placeUnited Kingdomen_US

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