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Article: Heterologous expression analyses of rice OsCAS in Arabidopsis and in yeast provide evidence for its roles in cyanide detoxification rather than in cysteine synthesis in vivo

TitleHeterologous expression analyses of rice OsCAS in Arabidopsis and in yeast provide evidence for its roles in cyanide detoxification rather than in cysteine synthesis in vivo
Authors
Issue Date2009
PublisherOxford University Press. The Journal's web site is located at http://jxb.oxfordjournals.org/
Citation
Journal Of Experimental Botany, 2009, v. 60 n. 3, p. 993-1008 How to Cite?
AbstractWhile most dicot plants produce little ethylene in their vegetative stage, many monocots such as rice liberate a relatively large amount of ethylene with cyanide as a co-product in their seedling stage when etiolated. One of the known functions of β-cyanoalanine synthase (CAS) is to detoxify the co-product cyanide during ethylene biosynthesis in higher plants. Based on a tryptic peptide sequence obtained from a partially purified CAS activity protein preparation in etiolated rice seedlings, the full-length putative rice CAS-encoding cDNA sequence (OsCAS), which is homologous to those O-acetylserine sulphydrylase (OASS) genes, was cloned. Unlike most of the CAS genes reported from dicots, the transcription of OsCAS is promoted by auxins but suppressed by ethylene. To address the function and the subcellular localization of this gene product in planta, a binary vector construct consisting of this gene appended with a yellow fluorescent protein-encoding sequence was employed to transform Arabidopsis. Specific activities on CAS and OASS of the purified recombinant protein from transgenic Arabidopsis were 181.04 μmol H 2S mg -1 protein min -1 and 0.92 μmol Cys mg -1 protein min -1, respectively, indicating that OsCAS favours CAS activity. The subcellular localization of OsCAS was found mostly in the mitochondria by immunogold electron-microscopy. Chemical cross-linking and in-gel assay on a heterodimer composed of functional and non-functional mutants in a yeast expression system on OsCAS suggested that OsCAS functions as a homodimer, similar to that of OASS. Despite the structural similarity of OsCAS with OASS, it has also been confirmed that OsCAS could not interact with serine-acetyltransferase, indicating that OsCAS mainly functions in cyanide detoxification. © 2009 The Author(s).
Persistent Identifierhttp://hdl.handle.net/10722/179121
ISSN
2015 Impact Factor: 5.677
2015 SCImago Journal Rankings: 2.798
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLai, KWen_US
dc.contributor.authorYau, CPen_US
dc.contributor.authorTse, YCen_US
dc.contributor.authorJiang, Len_US
dc.contributor.authorYip, WKen_US
dc.date.accessioned2012-12-19T09:52:08Z-
dc.date.available2012-12-19T09:52:08Z-
dc.date.issued2009en_US
dc.identifier.citationJournal Of Experimental Botany, 2009, v. 60 n. 3, p. 993-1008en_US
dc.identifier.issn0022-0957en_US
dc.identifier.urihttp://hdl.handle.net/10722/179121-
dc.description.abstractWhile most dicot plants produce little ethylene in their vegetative stage, many monocots such as rice liberate a relatively large amount of ethylene with cyanide as a co-product in their seedling stage when etiolated. One of the known functions of β-cyanoalanine synthase (CAS) is to detoxify the co-product cyanide during ethylene biosynthesis in higher plants. Based on a tryptic peptide sequence obtained from a partially purified CAS activity protein preparation in etiolated rice seedlings, the full-length putative rice CAS-encoding cDNA sequence (OsCAS), which is homologous to those O-acetylserine sulphydrylase (OASS) genes, was cloned. Unlike most of the CAS genes reported from dicots, the transcription of OsCAS is promoted by auxins but suppressed by ethylene. To address the function and the subcellular localization of this gene product in planta, a binary vector construct consisting of this gene appended with a yellow fluorescent protein-encoding sequence was employed to transform Arabidopsis. Specific activities on CAS and OASS of the purified recombinant protein from transgenic Arabidopsis were 181.04 μmol H 2S mg -1 protein min -1 and 0.92 μmol Cys mg -1 protein min -1, respectively, indicating that OsCAS favours CAS activity. The subcellular localization of OsCAS was found mostly in the mitochondria by immunogold electron-microscopy. Chemical cross-linking and in-gel assay on a heterodimer composed of functional and non-functional mutants in a yeast expression system on OsCAS suggested that OsCAS functions as a homodimer, similar to that of OASS. Despite the structural similarity of OsCAS with OASS, it has also been confirmed that OsCAS could not interact with serine-acetyltransferase, indicating that OsCAS mainly functions in cyanide detoxification. © 2009 The Author(s).en_US
dc.languageengen_US
dc.publisherOxford University Press. The Journal's web site is located at http://jxb.oxfordjournals.org/en_US
dc.relation.ispartofJournal of Experimental Botanyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshArabidopsis - Genetics - Metabolism - Ultrastructureen_US
dc.subject.meshBacterial Proteins - Metabolismen_US
dc.subject.meshCyanides - Metabolismen_US
dc.subject.meshCysteine - Biosynthesisen_US
dc.subject.meshEthylenes - Biosynthesisen_US
dc.subject.meshGene Expression Regulation, Planten_US
dc.subject.meshImmunoprecipitationen_US
dc.subject.meshKineticsen_US
dc.subject.meshLuminescent Proteins - Metabolismen_US
dc.subject.meshLyases - Chemistry - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshMetabolic Detoxication, Drugen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOryza Sativa - Enzymology - Geneticsen_US
dc.subject.meshPlant Roots - Ultrastructureen_US
dc.subject.meshPlants, Genetically Modifieden_US
dc.subject.meshProtein Transporten_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae - Genetics - Metabolismen_US
dc.subject.meshSeedling - Enzymology - Geneticsen_US
dc.subject.meshSequence Alignmenten_US
dc.titleHeterologous expression analyses of rice OsCAS in Arabidopsis and in yeast provide evidence for its roles in cyanide detoxification rather than in cysteine synthesis in vivoen_US
dc.typeArticleen_US
dc.identifier.emailYip, WK: wkyip@hkucc.hku.hken_US
dc.identifier.authorityYip, WK=rp00833en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1093/jxb/ern343en_US
dc.identifier.pmid19181864-
dc.identifier.scopuseid_2-s2.0-62349118389en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-62349118389&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume60en_US
dc.identifier.issue3en_US
dc.identifier.spage993en_US
dc.identifier.epage1008en_US
dc.identifier.eissn1460-2431-
dc.identifier.isiWOS:000264189900025-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridLai, KW=41361524000en_US
dc.identifier.scopusauthoridYau, CP=7007038455en_US
dc.identifier.scopusauthoridTse, YC=22941836600en_US
dc.identifier.scopusauthoridJiang, L=7403475889en_US
dc.identifier.scopusauthoridYip, WK=7102784428en_US
dc.identifier.citeulike4177166-

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