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Article: Characterization and function of a sunflower (Helianthus annuus L.) Class II acyl-CoA-binding protein

TitleCharacterization and function of a sunflower (Helianthus annuus L.) Class II acyl-CoA-binding protein
Authors
KeywordsAcyl-CoA
Acyl-CoA-binding protein
Oilseeds
Phosphatidylcholine
Phospholipids
Issue Date2020
PublisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/plantsci
Citation
Plant Science, 2020, v. 300, p. article no. 110630 How to Cite?
AbstractAcyl-CoA-binding proteins (ACBP) bind to long-chain acyl-CoA esters and phospholipids, enhancing the activity of different acyltransferases in animals and plants. Nevertheless, the role of these proteins in the synthesis of triacylglycerols (TAGs) remains unclear. Here, we cloned a cDNA encoding HaACBP1, a Class II ACBP from sunflower (Helianthus annuus), one of the world’s most important oilseed crop plants. Transcriptome analysis of this gene revealed strong expression in developing seeds from 16 to 30 days after flowering. The recombinant protein (rHaACBP1) was expressed in Escherichia coli and purified to be studied by in vitro isothermal titration calorimetry and for phospholipid binding. Its high affinity for saturated palmitoyl-CoA (16:0-CoA; KD 0.11 μM) and stearoyl-CoA (18:0-CoA; KD 0.13 μM) esters suggests that rHaACBP1 could act in acyl-CoA transfer pathways that involve saturated acyl derivatives. Furthermore, rHaACBP1 also binds to both oleoyl-CoA (18:1-CoA; KD 6.4 μM) and linoleoyl-CoA (18:2-CoA; KD 21.4 μM) esters, the main acyl-CoA substrates used to synthesise the TAGs that accumulate in sunflower seeds. Interestingly, rHaACBP1 also appears to bind to different species of phosphatidylcholines (dioleoyl-PC and dilinoleoyl-PC), glycerolipids that are also involved in TAG synthesis, and while it interacts with dioleoyl-PA, this is less prominent than its binding to the PC derivative. Expression of rHaACBP in yeast alters its fatty acid composition, as well as the composition and size of the host acyl-CoA pool. These results suggest that HaACBP1 may potentially fulfil a role in the transport and trafficking of acyl-CoAs during sunflower seed development.
Descriptionlink_to_subscribed_fulltext
Persistent Identifierhttp://hdl.handle.net/10722/290058
ISSN
2020 Impact Factor: 4.729
2020 SCImago Journal Rankings: 1.508
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorAznar-Moreno, JA-
dc.contributor.authorVenegas-Calerón, M-
dc.contributor.authorDu, ZY-
dc.contributor.authorGarcés, R-
dc.contributor.authorTanner, JA-
dc.contributor.authorChye, ML-
dc.contributor.authorMartínez-Force, E-
dc.date.accessioned2020-10-22T08:21:29Z-
dc.date.available2020-10-22T08:21:29Z-
dc.date.issued2020-
dc.identifier.citationPlant Science, 2020, v. 300, p. article no. 110630-
dc.identifier.issn0168-9452-
dc.identifier.urihttp://hdl.handle.net/10722/290058-
dc.descriptionlink_to_subscribed_fulltext-
dc.description.abstractAcyl-CoA-binding proteins (ACBP) bind to long-chain acyl-CoA esters and phospholipids, enhancing the activity of different acyltransferases in animals and plants. Nevertheless, the role of these proteins in the synthesis of triacylglycerols (TAGs) remains unclear. Here, we cloned a cDNA encoding HaACBP1, a Class II ACBP from sunflower (Helianthus annuus), one of the world’s most important oilseed crop plants. Transcriptome analysis of this gene revealed strong expression in developing seeds from 16 to 30 days after flowering. The recombinant protein (rHaACBP1) was expressed in Escherichia coli and purified to be studied by in vitro isothermal titration calorimetry and for phospholipid binding. Its high affinity for saturated palmitoyl-CoA (16:0-CoA; KD 0.11 μM) and stearoyl-CoA (18:0-CoA; KD 0.13 μM) esters suggests that rHaACBP1 could act in acyl-CoA transfer pathways that involve saturated acyl derivatives. Furthermore, rHaACBP1 also binds to both oleoyl-CoA (18:1-CoA; KD 6.4 μM) and linoleoyl-CoA (18:2-CoA; KD 21.4 μM) esters, the main acyl-CoA substrates used to synthesise the TAGs that accumulate in sunflower seeds. Interestingly, rHaACBP1 also appears to bind to different species of phosphatidylcholines (dioleoyl-PC and dilinoleoyl-PC), glycerolipids that are also involved in TAG synthesis, and while it interacts with dioleoyl-PA, this is less prominent than its binding to the PC derivative. Expression of rHaACBP in yeast alters its fatty acid composition, as well as the composition and size of the host acyl-CoA pool. These results suggest that HaACBP1 may potentially fulfil a role in the transport and trafficking of acyl-CoAs during sunflower seed development.-
dc.languageeng-
dc.publisherElsevier Ireland Ltd. The Journal's web site is located at http://www.elsevier.com/locate/plantsci-
dc.relation.ispartofPlant Science-
dc.subjectAcyl-CoA-
dc.subjectAcyl-CoA-binding protein-
dc.subjectOilseeds-
dc.subjectPhosphatidylcholine-
dc.subjectPhospholipids-
dc.titleCharacterization and function of a sunflower (Helianthus annuus L.) Class II acyl-CoA-binding protein-
dc.typeArticle-
dc.identifier.emailTanner, JA: jatanner@hkucc.hku.hk-
dc.identifier.authorityTanner, JA=rp00495-
dc.identifier.doi10.1016/j.plantsci.2020.110630-
dc.identifier.pmid33180709-
dc.identifier.scopuseid_2-s2.0-85090004834-
dc.identifier.hkuros317002-
dc.identifier.hkuros322301-
dc.identifier.volume300-
dc.identifier.spagearticle no. 110630-
dc.identifier.epagearticle no. 110630-
dc.identifier.isiWOS:000581184300010-
dc.publisher.placeIreland-
dc.identifier.issnl0168-9452-

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