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Article: Arabidopsis ACBP6 is an acyl-CoA-binding protein associated with phospholipid metabolism

TitleArabidopsis ACBP6 is an acyl-CoA-binding protein associated with phospholipid metabolism
Authors
KeywordsAcyl-CoA-binding protein
Freezing tolerance
Phosphatidylcholine-binding
phospholipid transfer
Issue Date2008
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/psb
Citation
Plant Signaling And Behavior, 2008, v. 3 n. 11, p. 1019-1020 How to Cite?
AbstractIn our recent paper in Plant Physiology, we showed that the Arabidopsis thaliana 10-kD acyl-CoA-binding protein, ACBP6, is subcellularly localized to the cytosol and that the overexpression of ACBP6 in transgenic Arabidopsis enhanced freezing tolerance. ACBP6-conferred freezing tolerance was independent of induced cold-regulated (COLD-RESPONSIVE) gene expression, but was correlated to an enhanced expression of phospholipase Dδ (PLDδ). Lipid analyses on cold-acclimated freezing-treated ACBP6-overexpressors revealed a decline in phosphatidylcholine (PC) and an elevation of phosphatidic acid (PA) in comparison to wild type. Furthermore, the His-tagged ACBP6 recombinant protein was observed using in vitro filter-binding assays to bind PC, but not PA or lysophosphatidylcholine. Taken together, our results implicate roles for ACBP6 in phospholipid metabolism that is related to gene regulation and PC-binding/transfer. This represents the first report demonstrating the in vitro binding of an ACBP to a phospholipid. The effect of ACBP6 on PLDδ expression is reminiscent of yeast 10-kD ACBP function in the regulation of genes associated with stress responses, fatty acid synthesis and phospholipid synthesis. However, the yeast ACBP regulates the expression of genes involved in phospholipid synthesis by donation of acyl-CoA esters and its binding to phospholipids remains to be demonstrated. ©2008 Landes Bioscience.
Persistent Identifierhttp://hdl.handle.net/10722/60721
ISSN
2015 SCImago Journal Rankings: 0.633
References

 

DC FieldValueLanguage
dc.contributor.authorChen, QFen_HK
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-05-31T04:17:08Z-
dc.date.available2010-05-31T04:17:08Z-
dc.date.issued2008en_HK
dc.identifier.citationPlant Signaling And Behavior, 2008, v. 3 n. 11, p. 1019-1020en_HK
dc.identifier.issn1559-2316en_HK
dc.identifier.urihttp://hdl.handle.net/10722/60721-
dc.description.abstractIn our recent paper in Plant Physiology, we showed that the Arabidopsis thaliana 10-kD acyl-CoA-binding protein, ACBP6, is subcellularly localized to the cytosol and that the overexpression of ACBP6 in transgenic Arabidopsis enhanced freezing tolerance. ACBP6-conferred freezing tolerance was independent of induced cold-regulated (COLD-RESPONSIVE) gene expression, but was correlated to an enhanced expression of phospholipase Dδ (PLDδ). Lipid analyses on cold-acclimated freezing-treated ACBP6-overexpressors revealed a decline in phosphatidylcholine (PC) and an elevation of phosphatidic acid (PA) in comparison to wild type. Furthermore, the His-tagged ACBP6 recombinant protein was observed using in vitro filter-binding assays to bind PC, but not PA or lysophosphatidylcholine. Taken together, our results implicate roles for ACBP6 in phospholipid metabolism that is related to gene regulation and PC-binding/transfer. This represents the first report demonstrating the in vitro binding of an ACBP to a phospholipid. The effect of ACBP6 on PLDδ expression is reminiscent of yeast 10-kD ACBP function in the regulation of genes associated with stress responses, fatty acid synthesis and phospholipid synthesis. However, the yeast ACBP regulates the expression of genes involved in phospholipid synthesis by donation of acyl-CoA esters and its binding to phospholipids remains to be demonstrated. ©2008 Landes Bioscience.en_HK
dc.languageengen_HK
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/psben_HK
dc.relation.ispartofPlant Signaling and Behavioren_HK
dc.subjectAcyl-CoA-binding proteinen_HK
dc.subjectFreezing toleranceen_HK
dc.subjectPhosphatidylcholine-bindingen_HK
dc.subjectphospholipid transferen_HK
dc.titleArabidopsis ACBP6 is an acyl-CoA-binding protein associated with phospholipid metabolismen_HK
dc.typeArticleen_HK
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityXiao, S=rp00817en_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.scopuseid_2-s2.0-56049123223en_HK
dc.identifier.hkuros154142en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-56049123223&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume3en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1019en_HK
dc.identifier.epage1020en_HK
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChen, QF=7406335399en_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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