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Article: Overexpression of the Arabidopsis 10-kilodalton acyl-coenzyme A-binding protein ACBP6 enhances freezing tolerance

TitleOverexpression of the Arabidopsis 10-kilodalton acyl-coenzyme A-binding protein ACBP6 enhances freezing tolerance
Authors
Issue Date2008
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 2008, v. 148 n. 1, p. 304-315 How to Cite?
AbstractSmall 10-kD acyl-coenzyme A-binding proteins (ACBPs) are highly conserved proteins that are prevalent in eukaryotes. In Arabidopsis (Arabidopsis thaliana), other than the 10-kDACBP homolog (designated Arabidopsis ACBP6), there are five larger forms of ACBPs ranging from 37.5 to 73.1 kD. In this study, the cytosolic subcellular localization of Arabidopsis ACBP6 was confirmed by analyses of transgenic Arabidopsis expressing autofluorescence-tagged ACBP6 and western-blot analysis of subcellular fractions using ACBP6-specific antibodies. The expression of Arabidopsis ACBP6 was noticeably induced at 48 h after 4°C treatment by northern-blot analysis and western-blot analysis. Furthermore, an acbp6 T-DNA insertional mutant that lacked ACBP6 mRNA and protein displayed increased sensitivity to freezing temperature (-8°C), while ACBP6-overexpressing transgenic Arabidopsis plants were conferred enhanced freezing tolerance. Northern-blot analysis indicated that ACBP6-associated freezing tolerance was not dependent on the induction of cold-regulated COLD-RESPONSIVE gene expression. Instead, ACBP6 overexpressors showed increased expression of mRNA encoding phospholipase Dδ. Lipid profiling analyses of rosettes from cold-acclimated, freezing-treated (-8°C) transgenic Arabidopsis plants overexpressing ACBP6 showed a decline in phosphatidylcholine (-36% and -46%) and an elevation of phosphatidic acid (73% and 67%) in comparison with wild-type plants. From our comparison, the gain in freezing tolerance in ACBP6 overexpressors that was accompanied by decreases in phosphatidylcholine and an accumulation of phosphatidic acid is consistent with previous findings on phospholipase Dδ-overexpressing transgenic Arabidopsis. In vitro filter-binding assays indicating that histidine-tagged ACBP6 binds phosphatidylcholine, but not phosphatidic acid or lysophosphatidylcholine, further imply a role for ACBP6 in phospholipid metabolism in Arabidopsis, including the possibility of ACBP6 in the cytosolic trafficking of phosphatidylcholine. © 2008 American Society of Plant Biologists.
Persistent Identifierhttp://hdl.handle.net/10722/179099
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChen, QFen_US
dc.contributor.authorXiao, Sen_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2012-12-19T09:51:58Z-
dc.date.available2012-12-19T09:51:58Z-
dc.date.issued2008en_US
dc.identifier.citationPlant Physiology, 2008, v. 148 n. 1, p. 304-315en_US
dc.identifier.issn0032-0889en_US
dc.identifier.urihttp://hdl.handle.net/10722/179099-
dc.description.abstractSmall 10-kD acyl-coenzyme A-binding proteins (ACBPs) are highly conserved proteins that are prevalent in eukaryotes. In Arabidopsis (Arabidopsis thaliana), other than the 10-kDACBP homolog (designated Arabidopsis ACBP6), there are five larger forms of ACBPs ranging from 37.5 to 73.1 kD. In this study, the cytosolic subcellular localization of Arabidopsis ACBP6 was confirmed by analyses of transgenic Arabidopsis expressing autofluorescence-tagged ACBP6 and western-blot analysis of subcellular fractions using ACBP6-specific antibodies. The expression of Arabidopsis ACBP6 was noticeably induced at 48 h after 4°C treatment by northern-blot analysis and western-blot analysis. Furthermore, an acbp6 T-DNA insertional mutant that lacked ACBP6 mRNA and protein displayed increased sensitivity to freezing temperature (-8°C), while ACBP6-overexpressing transgenic Arabidopsis plants were conferred enhanced freezing tolerance. Northern-blot analysis indicated that ACBP6-associated freezing tolerance was not dependent on the induction of cold-regulated COLD-RESPONSIVE gene expression. Instead, ACBP6 overexpressors showed increased expression of mRNA encoding phospholipase Dδ. Lipid profiling analyses of rosettes from cold-acclimated, freezing-treated (-8°C) transgenic Arabidopsis plants overexpressing ACBP6 showed a decline in phosphatidylcholine (-36% and -46%) and an elevation of phosphatidic acid (73% and 67%) in comparison with wild-type plants. From our comparison, the gain in freezing tolerance in ACBP6 overexpressors that was accompanied by decreases in phosphatidylcholine and an accumulation of phosphatidic acid is consistent with previous findings on phospholipase Dδ-overexpressing transgenic Arabidopsis. In vitro filter-binding assays indicating that histidine-tagged ACBP6 binds phosphatidylcholine, but not phosphatidic acid or lysophosphatidylcholine, further imply a role for ACBP6 in phospholipid metabolism in Arabidopsis, including the possibility of ACBP6 in the cytosolic trafficking of phosphatidylcholine. © 2008 American Society of Plant Biologists.en_US
dc.languageengen_US
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_US
dc.relation.ispartofPlant Physiologyen_US
dc.subject.meshAcclimatizationen_US
dc.subject.meshArabidopsis - Physiologyen_US
dc.subject.meshArabidopsis Proteins - Metabolismen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCold Temperatureen_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshFreezingen_US
dc.subject.meshGene Expression Regulation, Planten_US
dc.subject.meshLipid Metabolismen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshMutationen_US
dc.subject.meshPhosphatidylcholines - Metabolismen_US
dc.subject.meshPhospholipase D - Metabolismen_US
dc.subject.meshPlants, Genetically Modified - Physiologyen_US
dc.titleOverexpression of the Arabidopsis 10-kilodalton acyl-coenzyme A-binding protein ACBP6 enhances freezing toleranceen_US
dc.typeArticleen_US
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_US
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_US
dc.identifier.authorityXiao, S=rp00817en_US
dc.identifier.authorityChye, ML=rp00687en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1104/pp.108.123331en_US
dc.identifier.pmid18621979-
dc.identifier.scopuseid_2-s2.0-55549110935en_US
dc.identifier.hkuros154139-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-55549110935&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume148en_US
dc.identifier.issue1en_US
dc.identifier.spage304en_US
dc.identifier.epage315en_US
dc.identifier.isiWOS:000258947600027-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChen, QF=7406335399en_US
dc.identifier.scopusauthoridXiao, S=7402022635en_US
dc.identifier.scopusauthoridChye, ML=7003905460en_US
dc.identifier.citeulike4883975-

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