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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleFunctional and structural studies of the disulfide isomerase DsbC from the plant pathogen Xylella fastidiosa reveals a redox-dependent oligomeric modulation in vitropt_BR
dc.contributor.authorSantos, Clelton A.pt_BR
dc.contributor.authorToledo, Marcelo A. S.pt_BR
dc.contributor.authorTrivella, Daniela B. B.pt_BR
dc.contributor.authorBeloti, Lilian L.pt_BR
dc.contributor.authorSchneider, Dilaine R. S.pt_BR
dc.contributor.authorSaraiva, Antonio M.pt_BR
dc.contributor.authorCrucello, Alinept_BR
dc.contributor.authorAzzoni, Adriano R.pt_BR
dc.contributor.authorSouza, Alessandra A.pt_BR
dc.contributor.authorAparicio, Ricardopt_BR
dc.contributor.authorSouza, Anete P.pt_BR
unicamp.authorSantos, Clelton A.pt_BR
unicamp.authorToledo, Marcelo A. S.pt_BR
unicamp.authorToledo, Marcelo A. S.pt_BR
unicamp.authorBeloti, Lilian L.pt_BR
unicamp.authorSchneider, Dilaine R. S.pt_BR
unicamp.authorSaraiva, Antonio M.pt_BR
unicamp.authorCrucello, Alinept_BR
unicamp.authorAzzoni, Adriano R.pt_BR
unicamp.authorAparicio, Ricardopt_BR
unicamp.authorSouza, Anete P.pt_BR
unicamp.author.externalTrivella, Daniela B. B.pt
unicamp.author.externalBeloti, Lilian L.pt
unicamp.author.externalSchneider, Dilaine R. S.pt
unicamp.author.externalSaraiva, Antonio M.pt
unicamp.author.externalCrucello, Alinept
unicamp.author.externalAzzoni, Adriano R.pt
unicamp.author.externalSouza, Alessandra A.pt
unicamp.author.externalAparicio, Ricardopt
unicamp.author.externalSouza, Anete P.pt
dc.subjectbiofilm formationpt_BR
dc.subjectDsbCpt_BR
dc.subjectoligomeric assemblypt_BR
dc.subjectSAXSpt_BR
dc.subjectXylella fastidiosapt_BR
dc.subject.wosSMALL-ANGLE SCATTERINGpt_BR
dc.subject.wosX-RAY-SCATTERINGpt_BR
dc.subject.wosESCHERICHIA-COLI DSBCpt_BR
dc.subject.wosBOND FORMATIONpt_BR
dc.subject.wosCRYSTAL-STRUCTUREpt_BR
dc.subject.wosBIOFILM FORMATIONpt_BR
dc.subject.wosGENE-EXPRESSIONpt_BR
dc.subject.wosTHIOREDOXINpt_BR
dc.subject.wosPROTEINSpt_BR
dc.subject.wosISOMERIZATIONpt_BR
dc.description.abstractXylella fastidiosa is a Gram-negative bacterium that grows as a biofilm inside the xylem vessels of susceptible plants and causes several economically relevant crop diseases. In the present study, we report the functional and low-resolution structural characterization of the X. fastidiosa disulfide isomerase DsbC (XfDsbC). DsbC is part of the disulfide bond reduction/isomerization pathway in the bacterial periplasm and plays an important role in oxidative protein folding. In the present study, we demonstrate the presence of XfDsbC during different stages of X. fastidiosa biofilm development. XfDsbC was not detected during X. fastidiosa planktonic growth; however, after administering a sublethal copper shock, we observed an overexpression of XfDsbC that also occurred during planktonic growth. These results suggest that X. fastidiosa can use XfDsbC in vivo under oxidative stress conditions similar to those induced by copper. In addition, using dynamic light scattering and small-angle X-ray scattering, we observed that the oligomeric state of XfDsbC in vitro may be dependent on the redox environment. Under reducing conditions, XfDsbC is present as a dimer, whereas a putative tetrameric form was observed under nonreducing conditions. Taken together, our findings demonstrate the overexpression of XfDsbC during biofilm formation and provide the first structural model of a bacterial disulfide isomerase in solution. Structured digital abstract XfDsbC and XfDsbC bind by x ray scattering (View Interaction: 1, 2) XfDsbC and XfDsbC bind by molecular sieving (View interaction) XfDsbC and XfDsbC bind by comigration in non denaturing gel electrophoresis (View interaction) XfDsbC and XfDsbC bind by cross-linking study (View Interaction: 1, 2) XfDsbC and XfDsbC bind by dynamic light scattering (View Interaction: 1, 2)pt
dc.relation.ispartofFebs Journalpt_BR
dc.publisher.cityHobokenpt_BR
dc.publisherWiley-Blackwellpt_BR
dc.date.issued2012pt_BR
dc.identifier.citationFebs Journal. Wiley-Blackwell, v.279, n.20, p.3828-3843, 2012pt_BR
dc.language.isoengpt_BR
dc.description.volume279pt_BR
dc.description.issuenumber20pt_BR
dc.description.firstpage3828pt_BR
dc.description.lastpage3843pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1742-464Xpt_BR
dc.identifier.wosidWOS:000309447400006pt_BR
dc.identifier.doi10.1111/j.1742-4658.2012.08743.xpt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)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.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.date.available2013-09-19T18:06:52Z
dc.date.available2016-06-21T13:07:04Z-
dc.date.accessioned2013-09-19T18:06:52Z
dc.date.accessioned2016-06-21T13:07:04Z-
dc.description.provenanceMade available in DSpace on 2013-09-19T18:06:52Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.description.provenanceMade available in DSpace on 2016-06-21T13:07:04Z (GMT). No. of bitstreams: 0 Previous issue date: 2012en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/2482
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/2482-
dc.contributor.departmentGenética e Bioagentes
dc.contributor.unidadeCBMEGpt
Appears in Collections:CBMEG - Artigos e Outros Documentos

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