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Article: Depletion of the membrane-associated acyl-coenzyme a-binding protein ACBP1 enhances the ability of cold acclimation in Arabidopsis

TitleDepletion of the membrane-associated acyl-coenzyme a-binding protein ACBP1 enhances the ability of cold acclimation in Arabidopsis
Authors
Issue Date2010
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 2010, v. 152 n. 3, p. 1585-1597 How to Cite?
AbstractIn Arabidopsis (Arabidopsis thaliana), a family of six genes encodes acyl-coenzyme A-binding proteins (ACBPs). A member of this family, ACBP1, contains an amino-terminal transmembrane domain that targets it to the plasma membrane and the endoplasmic reticulum. To investigate ACBP1 function, ACBP1-overexpressing transgenic Arabidopsis plants were characterized using lipid analysis. ACBP1 overexpressors showed reduction in several species of diunsaturated phosphatidylcholine (PC), prompting us to investigate if they were altered in response to freezing stress. ACBP1 overexpressors demonstrated increased freezing sensitivity accompanied by a decrease in PC and an increase in phosphatidic acid (PA), while acbp1 mutant plants showed enhanced freezing tolerance associated with PC accumulation and PA reduction. We also showed binding of a recombinant eukaryotic ACBP (ACBP1) to PA, indicative of the possibility of enhanced PA interaction in ACBP1 over-expressors. Since phospholipase Da1 (PLDa1) is a major enzyme promoting the hydrolysis of PC to PA, PLDa1 expression was examined and was observed to be higher in ACBP1 overexpressors than in acbp1 mutant plants. In contrast, the expression of PLDd, which plays a positive role in freezing tolerance, declined in the ACBP1 overexpressors but increased in acbp1 mutant plants. Given that ACBP1 is localized to the endoplasmic reticulum and plasma membrane, it may regulate the expression of PLDa1 and PLDd by maintaining a membrane-associated PA pool through its ability to bind PA. Moreover, both genotypes showed no alterations in proline and soluble sugar content or in cold-regulated (COR6.6 and COR47) gene expression, suggesting that the ACBP1-mediated response is PLD associated and is independent of osmolyte accumulation. © 2010 American Society of Plant Biologists.
Persistent Identifierhttp://hdl.handle.net/10722/179184
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDu, ZYen_US
dc.contributor.authorXiao, Sen_US
dc.contributor.authorChen, QFen_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2012-12-19T09:52:38Z-
dc.date.available2012-12-19T09:52:38Z-
dc.date.issued2010en_US
dc.identifier.citationPlant Physiology, 2010, v. 152 n. 3, p. 1585-1597en_US
dc.identifier.issn0032-0889en_US
dc.identifier.urihttp://hdl.handle.net/10722/179184-
dc.description.abstractIn Arabidopsis (Arabidopsis thaliana), a family of six genes encodes acyl-coenzyme A-binding proteins (ACBPs). A member of this family, ACBP1, contains an amino-terminal transmembrane domain that targets it to the plasma membrane and the endoplasmic reticulum. To investigate ACBP1 function, ACBP1-overexpressing transgenic Arabidopsis plants were characterized using lipid analysis. ACBP1 overexpressors showed reduction in several species of diunsaturated phosphatidylcholine (PC), prompting us to investigate if they were altered in response to freezing stress. ACBP1 overexpressors demonstrated increased freezing sensitivity accompanied by a decrease in PC and an increase in phosphatidic acid (PA), while acbp1 mutant plants showed enhanced freezing tolerance associated with PC accumulation and PA reduction. We also showed binding of a recombinant eukaryotic ACBP (ACBP1) to PA, indicative of the possibility of enhanced PA interaction in ACBP1 over-expressors. Since phospholipase Da1 (PLDa1) is a major enzyme promoting the hydrolysis of PC to PA, PLDa1 expression was examined and was observed to be higher in ACBP1 overexpressors than in acbp1 mutant plants. In contrast, the expression of PLDd, which plays a positive role in freezing tolerance, declined in the ACBP1 overexpressors but increased in acbp1 mutant plants. Given that ACBP1 is localized to the endoplasmic reticulum and plasma membrane, it may regulate the expression of PLDa1 and PLDd by maintaining a membrane-associated PA pool through its ability to bind PA. Moreover, both genotypes showed no alterations in proline and soluble sugar content or in cold-regulated (COR6.6 and COR47) gene expression, suggesting that the ACBP1-mediated response is PLD associated and is independent of osmolyte accumulation. © 2010 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.meshAcclimatization - Geneticsen_US
dc.subject.meshArabidopsis - Genetics - Metabolismen_US
dc.subject.meshArabidopsis Proteins - Genetics - Metabolismen_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshCold Temperatureen_US
dc.subject.meshGene Expression Regulation, Planten_US
dc.subject.meshGene Knockout Techniquesen_US
dc.subject.meshPhosphatidic Acids - Metabolismen_US
dc.subject.meshPhosphatidylcholines - Metabolismen_US
dc.subject.meshPhospholipase D - Genetics - Metabolismen_US
dc.subject.meshPlants, Genetically Modified - Genetics - Metabolismen_US
dc.titleDepletion of the membrane-associated acyl-coenzyme a-binding protein ACBP1 enhances the ability of cold acclimation in Arabidopsisen_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.109.147066en_US
dc.identifier.pmid20107029-
dc.identifier.pmcidPMC2832255-
dc.identifier.scopuseid_2-s2.0-77949497907en_US
dc.identifier.hkuros170509-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77949497907&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume152en_US
dc.identifier.issue3en_US
dc.identifier.spage1585en_US
dc.identifier.epage1597en_US
dc.identifier.isiWOS:000276329500037-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDu, ZY=36150734700en_US
dc.identifier.scopusauthoridXiao, S=7402022635en_US
dc.identifier.scopusauthoridChen, QF=7406335399en_US
dc.identifier.scopusauthoridChye, ML=7003905460en_US
dc.identifier.citeulike6611669-

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