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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleSuspension cell culture as a tool for the characterization of class III peroxidases in sugarcanept_BR
dc.contributor.authorCesarino, Ipt_BR
dc.contributor.authorAraujo, Ppt_BR
dc.contributor.authorLeme, AFPpt_BR
dc.contributor.authorCreste, Spt_BR
dc.contributor.authorMazzafera, Ppt_BR
unicamp.author.emailpmazza@unicamp.brpt_BR
unicamp.authorCesarino, Igor Araujo, Pedro Mazzafera, Paulo Univ Estadual Campinas, Inst Biol, Dept Biol Vegetal, BR-13083970 Campinas, SP, Brazilpt_BR
unicamp.authorPaes Leme, Adriana Franco Lab Nacl Biociencias CNPEM ABTLuS, Campinas, SP, Brazilpt_BR
unicamp.authorCreste, Silvana Inst Agron Campinas, Ctr Cana, BR-14001970 Ribeirao Preto, SP, Brazilpt_BR
dc.subjectSuspension cell culturespt_BR
dc.subjectClass III peroxidasespt_BR
dc.subjectLigninpt_BR
dc.subjectProteomicspt_BR
dc.subjectGene expression analysispt_BR
dc.subject.wosArabidopsis-thalianapt_BR
dc.subject.wosLignin Biosynthesispt_BR
dc.subject.wosGene-expressionpt_BR
dc.subject.wosSyringyl Peroxidasespt_BR
dc.subject.wosPlant Peroxidasespt_BR
dc.subject.wosZinnia-eleganspt_BR
dc.subject.wosWallpt_BR
dc.subject.wosLignificationpt_BR
dc.subject.wosIdentificationpt_BR
dc.subject.wosElectrophoresispt_BR
dc.description.abstractSecreted class III peroxidases (EC 1.11.1.7) are implicated in a broad range of physiological processes throughout the plant life cycle. However, the unambiguous determination of the precise biological role of an individual class III peroxidase isoenzyme is still a difficult task due to genetic redundancy and broad substrate specificity in vitro. In addition, many difficulties are encountered during extraction and analysis of cell wall proteins. Since class III peroxidases are also secreted into the apoplast, the use of suspension cell cultures can facilitate isolation and functional characterization of individual isoforms. Here, we report on the characterization of class III peroxidases secreted in the spent medium of sugarcane suspension cell cultures. After treatment with specific inducers of cell wall lignification, peroxidases were isolated and activities assayed with guaiacol, syringaldazine and coniferyl alcohol. Enzymatic activity was not significantly different after treatments, regardless of the substrate, with the exception of methyl-jasmonate treatment, which led to a decreased guaiacol peroxidase activity. Remarkably, peroxidases isolated from the medium were capable of oxidizing syringaldazine, an analog to sinapyl alcohol, suggesting that sugarcane cultures can produce peroxidases putatively correlated to lignification. A proteomic approach using activity staining of 2-DE gels revealed a complex isoperoxidase profile, composed predominantly of cationic isoforms. Individual spots were excised and analyzed by LC-ESI-Q-TOF and homology-based search against the Sugarcane EST Database resulted in the identification of several proteins. Spatio-temporal expression pattern of selected genes was determined for validation of identified class III peroxidases that were preferentially expressed during sugarcane stem development. (C) 2012 Elsevier Masson SAS. All rights reserved.pt
dc.relation.ispartofPlant Physiology And Biochemistrypt_BR
dc.relation.ispartofabbreviationPlant Physiol. Biochem.pt_BR
dc.publisher.cityParispt_BR
dc.publisher.countryFrançapt_BR
dc.publisherElsevier France-editions Scientifiques Medicales Elsevierpt_BR
dc.date.issued2013pt_BR
dc.date.monthofcirculationJANpt_BR
dc.identifier.citationPlant Physiology And Biochemistry. Elsevier France-editions Scientifiques Medicales Elsevier, v. 62, n. 1, n. 10, 2013.pt_BR
dc.language.isoenpt_BR
dc.description.volume62pt_BR
dc.description.firstpage1pt_BR
dc.description.lastpage10pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
unicamp.cruespUSPpt_BR
dc.identifier.issn0981-9428pt_BR
dc.identifier.wosidWOS:000314134600001pt_BR
dc.identifier.doi10.1016/j.plaphy.2012.10.015pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsordocumentnumberFAPESP [BIOEN 08/58035-6]pt
dc.date.available2014-07-30T19:51:44Z
dc.date.available2015-11-26T16:56:40Z-
dc.date.accessioned2014-07-30T19:51:44Z
dc.date.accessioned2015-11-26T16:56:40Z-
dc.description.provenanceMade available in DSpace on 2014-07-30T19:51:44Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
dc.description.provenanceMade available in DSpace on 2015-11-26T16:56:40Z (GMT). No. of bitstreams: 0 Previous issue date: 2013en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/73955
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/73955-
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