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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampSantiago, André da Silvapt_BR
dc.contributor.authorunicampMendes, Juliano Salespt_BR
dc.contributor.authorunicampSantos, Clelton Aparecido dospt_BR
dc.contributor.authorunicampToledo, Marcelo Augusto Szymanski dept_BR
dc.contributor.authorunicampBeloti, Lilian Luziapt_BR
dc.contributor.authorunicampCrucello, Alinept_BR
dc.contributor.authorunicampCrivelente Horta, Maria Augustapt_BR
dc.contributor.authorunicampFavaro, Marianna Teixeira de Pinhopt_BR
dc.contributor.authorunicampMurillo Munar, Duber Marcelpt_BR
dc.contributor.authorunicampCotta, Mônica Alonsopt_BR
dc.contributor.authorunicampSouza, Anete Pereira dept_BR
dc.typeArtigopt_BR
dc.titleThe Antitoxin Protein Of A Toxin-antitoxin System From Xylella Fastidiosa Is Secreted Via Outer Membrane Vesiclesen
dc.titleThe antitoxin protein of a toxin-antitoxin system from Xylella fastidiosa is secreted via outer membrane vesiclespt_BR
dc.contributor.authorSantiago, A. da S.pt_BR
dc.contributor.authorMendes, J. S.pt_BR
dc.contributor.authorSantos, C. A. dospt_BR
dc.contributor.authorToledo, M. A. S. dept_BR
dc.contributor.authorBeloti, L. L.pt_BR
dc.contributor.authorCrucello, A.pt_BR
dc.contributor.authorHorta, M. A. C.pt_BR
dc.contributor.authorFavaro, M. T. de P.pt_BR
dc.contributor.authorMunar, D. M. M.pt_BR
dc.contributor.authorSouza, A. A. dept_BR
dc.contributor.authorCotta, M. A.pt_BR
dc.contributor.authorSouza, A. P. dept_BR
dc.subjectXylella Fastidiosaen
dc.subjectProtein Characterizationen
dc.subjectToxin-antitoxin Systemen
dc.subjectOmven
dc.subjectBiofilmen
dc.subjectXylella fastidiosa, Caracterização de proteínas, Biofilmespt_BR
dc.subject.otherlanguageXylella fastidiosa, Protein characterization, Biofilmspt_BR
dc.description.abstractThe Xylella fastidiosa subsp pauca strain 9a5c is a Gram-negative, xylem-limited bacterium that is able to form a biofilm and affects citrus crops in Brazil. Some genes are considered to be involved in biofilm formation, but the specific mechanisms involved in this process remain unknown. This limited understanding of how some bacteria form biofilms is a major barrier to our comprehension of the progression of diseases caused by biofilm-producing bacteria. Several investigations have shown that the toxin-antitoxin (TA) operon is related to biofilm formation. This operon is composed of a toxin with RNAse activity and its cognate antitoxin. Previous reports have indicated that the antitoxin is able to inhibit toxin activity and modulate the expression of the operon as well as other target genes involved in oxidative stress and mobility. In this study, we characterize a toxin antitoxin system consisting of XfMqsR and XfYgiT, respectively, from X. fastidiosa subsp. pauca strain 9a5c. These proteins display a high similarity to their homologs in X fastidiosa strain Temecula and a predicted tridimensional structure that is similar to MqsR-YgiT from Escherichia coli, The characterization was performed using in vitro assays such as analytical ultracentrifugation (AUC), size exclusion chromatography, isothermal titration calorimetry, and Western blotting. Using a fluorometric assay to detect RNAses, we demonstrated that XfMqsR is thermostable and can degrade RNA. XfMqsR is inhibited by XfYgiT, which interacts with its own promoter. XfYgiT is known to be localized in the intracellular compartment; however, we provide strong evidence that X. fastidiosa secretes wild-type XfYgiT into the extracellular environment via outer membrane vesicles, as confirmed by Western blotting and specific immunofluorescence labeling visualized by fluorescence microscopy. Taken together, our results characterize the TA system from X. fastidiosa strain 9a5c, and we also discuss the possible influence of wild-type XfYgiT in the cell.en
dc.description.abstractThe Xylella fastidiosa subsp pauca strain 9a5c is a Gram-negative, xylem-limited bacterium that is able to form a biofilm and affects citrus crops in Brazil. Some genes are considered to be involved in biofilm formation, but the specific mechanisms involved in this process remain unknown. This limited understanding of how some bacteria form biofilms is a major barrier to our comprehension of the progression of diseases caused by biofilm-producing bacteria. Several investigations have shown that the toxin-antitoxin (TA) operon is related to biofilm formation. This operon is composed of a toxin with RNAse activity and its cognate antitoxin. Previous reports have indicated that the antitoxin is able to inhibit toxin activity and modulate the expression of the operon as well as other target genes involved in oxidative stress and mobility. In this study, we characterize a toxin antitoxin system consisting of XfMqsR and XfYgiT, respectively, from X. fastidiosa subsp. pauca strain 9a5c. These proteins display a high similarity to their homologs in X fastidiosa strain Temecula and a predicted tridimensional structure that is similar to MqsR-YgiT from Escherichia coli, The characterization was performed using in vitro assays such as analytical ultracentrifugation (AUC), size exclusion chromatography, isothermal titration calorimetry, and Western blotting. Using a fluorometric assay to detect RNAses, we demonstrated that XfMqsR is thermostable and can degrade RNA. XfMqsR is inhibited by XfYgiT, which interacts with its own promoter. XfYgiT is known to be localized in the intracellular compartment, however, we provide strong evidence that X. fastidiosa secretes wild-type XfYgiT into the extracellular environment via outer membrane vesicles, as confirmed by Western blotting and specific immunofluorescence labeling visualized by fluorescence microscopy. Taken together, our results characterize the TA system from X. fastidiosa strain 9a5c, and we also discuss the possible influence of wild-type XfYgiT in the cell.pt_BR
dc.relation.ispartofFrontiers in microbiologypt_BR
dc.relation.ispartofabbreviationFront. microbiol.pt_BR
dc.publisher.cityLausannept_BR
dc.publisher.countrySuíçapt_BR
dc.publisherFrontiers Research Foundationpt_BR
dc.date.issued2016pt_BR
dc.date.monthofcirculationDec.pt_BR
dc.identifier.citationFrontiers In Microbiology. Frontiers Media Sa, v. 7, p. , 2016.pt_BR
dc.language.isoengpt_BR
dc.description.volume7pt_BR
dc.description.firstpage1pt_BR
dc.description.lastpage14pt_BR
dc.rightsabertopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn1664-302Xpt_BR
dc.identifier.eissn1664-302Xpt_BR
dc.identifier.doi10.3382/fmicb.2016.02030pt_BR
dc.identifier.urlhttps://www.frontiersin.org/articles/10.3389/fmicb.2016.02030pt_BR
dc.description.sponsorshipFAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOpt_BR
dc.description.sponsorshipCAPES - COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIORpt_BR
dc.description.sponsorshipCNPQ - CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOpt_BR
dc.description.sponsorship1FAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOpt_BR
dc.description.sponsorship1CAPES - COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIORpt_BR
dc.description.sponsorship1CNPQ - CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOpt_BR
dc.description.sponsordocumentnumber2011/50268-4pt_BR
dc.description.sponsordocumentnumberSem informaçãopt_BR
dc.description.sponsordocumentnumberSem informaçãopt_BR
dc.date.available2017-11-13T13:23:31Z-
dc.date.accessioned2017-11-13T13:23:31Z-
dc.description.provenanceMade available in DSpace on 2017-11-13T13:23:31Z (GMT). No. of bitstreams: 1 000390159100001.pdf: 3400426 bytes, checksum: 966315b751af5543fe8fb68074fe2f39 (MD5) Previous issue date: 2016 Bitstreams deleted on 2020-09-02T13:42:16Z: 000390159100001.pdf,. Added 1 bitstream(s) on 2020-09-02T13:46:35Z : No. of bitstreams: 1 000390159100001.pdf: 3216796 bytes, checksum: 3e617e8a15bf0b119cd9ea2310d59d7a (MD5)en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/328117-
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentCentro de Biologia Molecular e Engenharia Genéticapt_BR
dc.contributor.departmentDepartamento de Física Aplicadapt_BR
dc.contributor.departmentDepartamento de Física Aplicadapt_BR
dc.contributor.departmentDepartamento de Biologia Vegetalpt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Física Gleb Wataghinpt_BR
dc.contributor.unidadeInstituto de Física Gleb Wataghinpt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.subject.keywordToxin-antitoxin system, Outer membrane vesiclespt_BR
dc.identifier.source000390159100001pt_BR
dc.creator.orcidSem informaçãopt_BR
dc.creator.orcid0000-0001-7249-2292pt_BR
dc.creator.orcid0000-0002-6725-8925pt_BR
dc.creator.orcid0000-0003-4318-7381pt_BR
dc.creator.orcid0000-0002-7345-2847pt_BR
dc.creator.orcidSem informaçãopt_BR
dc.creator.orcid0000-0003-2159-5296pt_BR
dc.creator.orcid0000-0003-2942-247Xpt_BR
dc.creator.orcidSem informaçãopt_BR
dc.creator.orcid0000-0002-2779-5179pt_BR
dc.creator.orcid0000-0003-3831-9829pt_BR
dc.type.formArtigopt_BR
dc.identifier.articleid2030pt_BR
dc.description.sponsorNoteWe gratefully acknowledge the Laboratório de Espectroscopia e Calorimetria (LEC) and Laboratório Nacional de Biociências—LNBio (Campinas, Brazil) for their support with the circular dichroism assays and to the Brazilian Nanotechnology National Laboratory LNNano for helping us with the analysis of the AFM images and to the Field Emission Scanning Electron Microscopy—FESEM, Chemistry Institute, Unicamp, Campinas. Also, we are grateful to the staff of the Life Sciences Core Facility (LaCTAD) from the State University of Campinas (UNICAMP) for the ITC analysis. We also would like to thank to the professor Paulo Pinto Joazeiro of the Structural and Cell Biology Department of the Biology Institute from Unicamp. The authors gratefully acknowledge the Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP, Process 2012/51580-4 and 2001/07533-7) and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Computational Biology Program). ASS was partially supported by a Ph.D. fellowship from FAPESP (Process 2011/50268-4) and CAPES (Computational Biology Program), CS is the recipient of a postdoctoral fellowship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), and APS is the recipient of a research fellowship from CNPq.pt_BR
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