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Article: Characterization of a small acyl-CoA-binding protein (ACBP) from Helianthus annuus L. and its binding affinities

TitleCharacterization of a small acyl-CoA-binding protein (ACBP) from Helianthus annuus L. and its binding affinities
Authors
KeywordsAcyl-CoA
Acyl-CoA binding protein
Phosphatidic acid
Phosphatidylcholine
Phospholipids
Sunflower
Issue Date2016
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, 2016, v. 102, p. 141-150 How to Cite?
AbstractAcyl-CoA-binding proteins (ACBPs) bind to acyl-CoA esters and promote their interaction with other proteins, lipids and cell structures. Small class I ACBPs have been identified in different plants, such as Arabidopsis thaliana (AtACBP6), Brassica napus (BnACBP) and Oryza sativa (OsACBP1, OsACBP2, OsACBP3), and they are capable of binding to different acyl-CoA esters and phospholipids. Here we characterize HaACBP6, a class I ACBP expressed in sunflower (Helianthus annuus) tissues, studying the specificity of its corresponding recombinant HaACBP6 protein towards various acyl-CoA esters and phospholipids in vitro, particularly using isothermal titration calorimetry and protein phospholipid binding assays. This protein binds with high affinity to de novo synthetized derivatives palmitoly-CoA, stearoyl-CoA and oleoyl-CoA (Kd 0.29, 0.14 and 0.15 μM respectively). On the contrary, it showed lower affinity towards linoleoyl-CoA (Kd 5.6 μM). Moreover, rHaACBP6 binds to different phosphatidylcholine species (dipalmitoyl-PC, dioleoyl-PC and dilinoleoyl-PC), yet it displays no affinity towards other phospholipids like lyso-PC, phosphatidic acid and lysophosphatidic acid derivatives. In the light of these results, the possible involvement of this protein in sunflower oil synthesis is considered.
Persistent Identifierhttp://hdl.handle.net/10722/230265
ISSN
2015 Impact Factor: 2.928
2015 SCImago Journal Rankings: 1.167

 

DC FieldValueLanguage
dc.contributor.authorAznar-Moreno, JA-
dc.contributor.authorVenegas-Caleron, M-
dc.contributor.authorDu, ZY-
dc.contributor.authorGarces, R-
dc.contributor.authorTanner, JA-
dc.contributor.authorChye, ML-
dc.contributor.authorMartine-Force, E-
dc.contributor.authorSalas, JJ-
dc.date.accessioned2016-08-23T14:16:03Z-
dc.date.available2016-08-23T14:16:03Z-
dc.date.issued2016-
dc.identifier.citationPlant Physiology and Biochemistry, 2016, v. 102, p. 141-150-
dc.identifier.issn0981-9428-
dc.identifier.urihttp://hdl.handle.net/10722/230265-
dc.description.abstractAcyl-CoA-binding proteins (ACBPs) bind to acyl-CoA esters and promote their interaction with other proteins, lipids and cell structures. Small class I ACBPs have been identified in different plants, such as Arabidopsis thaliana (AtACBP6), Brassica napus (BnACBP) and Oryza sativa (OsACBP1, OsACBP2, OsACBP3), and they are capable of binding to different acyl-CoA esters and phospholipids. Here we characterize HaACBP6, a class I ACBP expressed in sunflower (Helianthus annuus) tissues, studying the specificity of its corresponding recombinant HaACBP6 protein towards various acyl-CoA esters and phospholipids in vitro, particularly using isothermal titration calorimetry and protein phospholipid binding assays. This protein binds with high affinity to de novo synthetized derivatives palmitoly-CoA, stearoyl-CoA and oleoyl-CoA (Kd 0.29, 0.14 and 0.15 μM respectively). On the contrary, it showed lower affinity towards linoleoyl-CoA (Kd 5.6 μM). Moreover, rHaACBP6 binds to different phosphatidylcholine species (dipalmitoyl-PC, dioleoyl-PC and dilinoleoyl-PC), yet it displays no affinity towards other phospholipids like lyso-PC, phosphatidic acid and lysophosphatidic acid derivatives. In the light of these results, the possible involvement of this protein in sunflower oil synthesis is considered.-
dc.languageeng-
dc.publisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/plaphy-
dc.relation.ispartofPlant Physiology and Biochemistry-
dc.rightsPosting accepted manuscript (postprint): © <year>. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.subjectAcyl-CoA-
dc.subjectAcyl-CoA binding protein-
dc.subjectPhosphatidic acid-
dc.subjectPhosphatidylcholine-
dc.subjectPhospholipids-
dc.subjectSunflower-
dc.titleCharacterization of a small acyl-CoA-binding protein (ACBP) from Helianthus annuus L. and its binding affinities-
dc.typeArticle-
dc.identifier.emailTanner, JA: jatanner@hku.hk-
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authorityTanner, JA=rp00495-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.plaphy.2016.02.025-
dc.identifier.pmid26938582-
dc.identifier.hkuros260380-
dc.identifier.volume102-
dc.identifier.spage141-
dc.identifier.epage150-
dc.publisher.placeFrance-

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