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Article: Acyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote tolerance to cadmium-induced oxidative stress in transgenic Arabidopsis

TitleAcyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote tolerance to cadmium-induced oxidative stress in transgenic Arabidopsis
Authors
KeywordsAcyl-CoA-binding protein
Cadmium
Hydrogen peroxide
Lysophospholipase
Oxidative stress
Zinc
Issue Date2010
PublisherWiley-Blackwell Publishing Ltd. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0960-7412
Citation
Plant Journal, 2010, v. 62 n. 6, p. 989-1003 How to Cite?
AbstractSummary Lysophospholipids are intermediates of phospholipid metabolism resulting from stress and lysophospholipases detoxify lysophosphatidylcholine (lysoPC). Many lysophospholipases have been characterized in mammals and bacteria, but few have been reported from plants. Arabidopsis thaliana lysophospholipase 2 (lysoPL2) (At1g52760) was identified as a protein interactor of acyl-CoA-binding protein 2 (ACBP2) in yeast two-hybrid analysis and co-immunoprecipitation assays. BLASTP analysis indicated that lysoPL2 showed ∼35% amino acid identity to the lysoPL1 family. Co-localization of autofluorescence-tagged lysoPL2 and ACBP2 by confocal microscopy in agroinfiltrated tobacco suggests the plasma membrane as a site for their subcellular interaction. LysoPL2 mRNA was induced by zinc (Zn) and hydrogen peroxide (H 2O 2), and lysoPL2 knockout mutants showed enhanced sensitivity to Zn and H 2O 2 in comparison to wild type. LysoPL2-overexpressing Arabidopsis was more tolerant to H 2O 2 and cadmium (Cd) than wild type, suggesting involvement of lysoPL2 in phospholipid repair following lipid peroxidation arising from metal-induced stress. Lipid hydroperoxide (LOOH) contents in ACBP2-overexpressors and lysoPL2-overexpressors after Cd-treatment were lower than wild type, indicating that ACBP2 and lysoPL2 confer protection during oxidative stress. A role for lysoPL2 in lysoPC detoxification was demonstrated when recombinant lysoPL2 was observed to degrade lysoPC in vitro. Filter-binding assays and Lipidex competition assays showed that (His) 6-ACBP2 binds lysoPC in vitro. Binding was disrupted in a (His) 6-ACBP2 derivative lacking the acyl-CoA-binding domain, confirming that this domain confers lysoPC binding. These results suggest that ACBP2 can bind both lysoPC and lysoPL2 to promote the degradation of lysoPC in response to Cd-induced oxidative stress. © 2010 Blackwell Publishing Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/124084
ISSN
2015 Impact Factor: 5.468
2015 SCImago Journal Rankings: 3.457
ISI Accession Number ID
Funding AgencyGrant Number
University Grants Committee of the Hong Kong Special Administrative Region, ChinaAoE/B-07/99
University of Hong Kong10208034
Funding Information:

We thank M.M. Goodin (UC Berkeley; pGDR), W.C. Yang (Institute of Genetics and Developmental Biology; pBI-eGFP), M. Frentzen (Institut fur Biologie, Aachen; BnLPAAT cDNA), W.K. Yip (provision of Biolistic PDS-1000/He system), G.S.W. Tsao (provision of Zeiss LSM510 META) and TAIR (lysoPL2 mutant seeds). This work was supported by the University Grants Committee of the Hong Kong Special Administrative Region, China (Project AoE/B-07/99) and University of Hong Kong (Grant 10208034, postdoctoral fellowship to SX and studentship to WG).

References

 

DC FieldValueLanguage
dc.contributor.authorGao, Wen_HK
dc.contributor.authorLi, HYen_HK
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-10-22T07:06:55Z-
dc.date.available2010-10-22T07:06:55Z-
dc.date.issued2010en_HK
dc.identifier.citationPlant Journal, 2010, v. 62 n. 6, p. 989-1003en_HK
dc.identifier.issn0960-7412en_HK
dc.identifier.urihttp://hdl.handle.net/10722/124084-
dc.description.abstractSummary Lysophospholipids are intermediates of phospholipid metabolism resulting from stress and lysophospholipases detoxify lysophosphatidylcholine (lysoPC). Many lysophospholipases have been characterized in mammals and bacteria, but few have been reported from plants. Arabidopsis thaliana lysophospholipase 2 (lysoPL2) (At1g52760) was identified as a protein interactor of acyl-CoA-binding protein 2 (ACBP2) in yeast two-hybrid analysis and co-immunoprecipitation assays. BLASTP analysis indicated that lysoPL2 showed ∼35% amino acid identity to the lysoPL1 family. Co-localization of autofluorescence-tagged lysoPL2 and ACBP2 by confocal microscopy in agroinfiltrated tobacco suggests the plasma membrane as a site for their subcellular interaction. LysoPL2 mRNA was induced by zinc (Zn) and hydrogen peroxide (H 2O 2), and lysoPL2 knockout mutants showed enhanced sensitivity to Zn and H 2O 2 in comparison to wild type. LysoPL2-overexpressing Arabidopsis was more tolerant to H 2O 2 and cadmium (Cd) than wild type, suggesting involvement of lysoPL2 in phospholipid repair following lipid peroxidation arising from metal-induced stress. Lipid hydroperoxide (LOOH) contents in ACBP2-overexpressors and lysoPL2-overexpressors after Cd-treatment were lower than wild type, indicating that ACBP2 and lysoPL2 confer protection during oxidative stress. A role for lysoPL2 in lysoPC detoxification was demonstrated when recombinant lysoPL2 was observed to degrade lysoPC in vitro. Filter-binding assays and Lipidex competition assays showed that (His) 6-ACBP2 binds lysoPC in vitro. Binding was disrupted in a (His) 6-ACBP2 derivative lacking the acyl-CoA-binding domain, confirming that this domain confers lysoPC binding. These results suggest that ACBP2 can bind both lysoPC and lysoPL2 to promote the degradation of lysoPC in response to Cd-induced oxidative stress. © 2010 Blackwell Publishing Ltd.en_HK
dc.languageeng-
dc.publisherWiley-Blackwell Publishing Ltd. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0960-7412en_HK
dc.relation.ispartofPlant Journalen_HK
dc.subjectAcyl-CoA-binding proteinen_HK
dc.subjectCadmiumen_HK
dc.subjectHydrogen peroxideen_HK
dc.subjectLysophospholipaseen_HK
dc.subjectOxidative stressen_HK
dc.subjectZincen_HK
dc.titleAcyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote tolerance to cadmium-induced oxidative stress in transgenic Arabidopsisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0960-7412&volume=62&issue=6&spage=989&epage=1003&date=2010&atitle=Acyl-CoA-binding+protein+2+binds+lysophospholipase+2+and+lysoPC+to+promote+tolerance+to+cadmium-induced+oxidative+stress+in+transgenic+Arabidopsis-
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.doi10.1111/j.1365-313X.2010.04209.xen_HK
dc.identifier.pmid20345607-
dc.identifier.scopuseid_2-s2.0-77953485056en_HK
dc.identifier.hkuros172645-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77953485056&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume62en_HK
dc.identifier.issue6en_HK
dc.identifier.spage989en_HK
dc.identifier.epage1003en_HK
dc.identifier.isiWOS:000278624700007-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridGao, W=36045713300en_HK
dc.identifier.scopusauthoridLi, HY=22953303900en_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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