Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/243787
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampRosalen, Pedro Luizpt_BR
dc.typeArtigopt_BR
dc.titleTranscriptional and phenotypic characterization of novel Spx-regulated genes in Streptococcus mutanspt_BR
dc.contributor.authorGalvão, Livia C. C.pt_BR
dc.contributor.authorMiller, James H.pt_BR
dc.contributor.authorKajfasz, Jessica K.pt_BR
dc.contributor.authorScott-Anne, Kathypt_BR
dc.contributor.authorFreires, Irlan A.pt_BR
dc.contributor.authorFranco, Gilson C. N.pt_BR
dc.contributor.authorAbranches Jacquelinept_BR
dc.contributor.authorRosalen, Pedro L.pt_BR
dc.contributor.authorLemos, José A.pt_BR
dc.subjectEstresse oxidativopt_BR
dc.subjectMetabolismo energéticopt_BR
dc.subject.otherlanguageOxidative stresspt_BR
dc.subject.otherlanguageEnergy metabolismpt_BR
dc.description.abstractIn oral biofilms, two of the major environmental challenges encountered by the dental pathogen Streptococcus mutans are acid and oxidative stresses. Previously, we showed that the S. mutans transcriptional regulators SpxA1 and SpxA2 (formerly SpxA and SpxB, respectively) are involved in stress survival by activating the expression of classic oxidative stress genes such as dpr, nox, sodA and tpx. We reasoned that some of the uncharacterized genes under SpxA1/A2 control are potentially involved in oxidative stress management. Therefore, the goal of this study was to use Spx-regulated genes as a tool to identify novel oxidative stress genes in S. mutans. Quantitative real-time PCR was used to evaluate the responses of ten Spx-regulated genes during H2O2 stress in the parent and Delta spx strains. Transcription activation of the H2O2-induced genes (8 out of 10) was strongly dependent on SpxA1 and, to a lesser extent, SpxA2. In vitro transcription assays revealed that one or both Spx proteins directly regulate three of these genes. The gene encoding the FeoB ferrous permease was slightly repressed by H2O2 but constitutively induced in strains lacking SpxA1. Nine genes were selected for downstream mutational analysis but inactivation of smu127, encoding a subunit of the acetoin dehydrogenase was apparently lethal. In vitro and in vivo characterization of the viable mutants indicated that, in addition to the transcriptional activation of reducing and antioxidant pathways, Spx performs an important role in iron homeostasis by regulating the intracellular availability of free iron. In particular, inactivation of the genes encoding the Fe-S biogenesis SUF system and the previously characterized iron-binding protein Dpr resulted in impaired growth under different oxidative stress conditions, increased sensitivity to iron and lower infectivity in rats. These results serve as an entryway into the characterization of novel genes and pathways that allow S. mutans to cope with oxidative stresspt
dc.relation.ispartofPLoS onept_BR
dc.relation.ispartofabbreviationPLoS onept_BR
dc.publisher.citySan Francisco, CApt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherPublic Library of Sciencept_BR
dc.date.issued2015pt_BR
dc.date.monthofcirculationApr.pt_BR
dc.identifier.citationTranscriptional And Phenotypic Characterization Of Novel Spx-regulated Genes In Streptococcus Mutans. Public Library Science, v. 10, p. APR-2015.pt_BR
dc.language.isoengpt_BR
dc.description.volume10pt_BR
dc.description.issuenumber4pt_BR
dc.rightsabertopt_BR
dc.sourceWOSpt_BR
dc.identifier.eissn1932-6203pt_BR
dc.identifier.doi10.1371/journal.pone.0124969pt_BR
dc.identifier.urlhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0124969pt_BR
dc.description.sponsorshipCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESpt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsorship1CAPES - COORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL E NÍVEL SUPERIORpt_BR
dc.description.sponsorship1FAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOpt_BR
dc.description.sponsordocumentnumberCAPES [6849-12-1]pt
dc.description.sponsordocumentnumberFAPESP [2012/032278-3, 2014/03816-4]pt
dc.description.sponsordocumentnumber6849-12-1pt_BR
dc.description.sponsordocumentnumber2012/032278-3; 2014/03816-4pt_BR
dc.date.available2016-06-07T13:33:47Z-
dc.date.accessioned2016-06-07T13:33:47Z-
dc.description.provenanceMade available in DSpace on 2016-06-07T13:33:47Z (GMT). No. of bitstreams: 1 wos_000353332000098.pdf: 840723 bytes, checksum: fe105af0d7512c0b31c7dae957b924f2 (MD5) Previous issue date: 2015 Bitstreams deleted on 2020-05-14T20:38:58Z: wos_000353332000098.pdf,. Added 1 bitstream(s) on 2020-05-14T20:43:18Z : No. of bitstreams: 1 000353332000098.pdf: 485382 bytes, checksum: 11da28fee113ebe4d50be08af3a1d6ee (MD5) Bitstreams deleted on 2020-06-04T12:48:16Z: 000353332000098.pdf,. Added 1 bitstream(s) on 2020-06-04T12:53:29Z : No. of bitstreams: 1 000353332000098.pdf: 1329776 bytes, checksum: e6bb9a8ba3c70dd13a8b587ccab76924 (MD5)en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/243787-
dc.contributor.departmentDepartamento de Ciências Fisiológicaspt_BR
dc.contributor.unidadeFaculdade de Odontologia de Piracicabapt_BR
dc.subject.keywordNadh oxidasept_BR
dc.subject.keywordRNA-polymerasept_BR
dc.subject.keywordIron binding proteinpt_BR
dc.subject.keywordAssembly systempt_BR
dc.subject.keywordEscherichia colipt_BR
dc.subject.keywordOxygen tolerancept_BR
dc.subject.keywordBacillus subtilispt_BR
dc.subject.keywordFerrous ironpt_BR
dc.identifier.source000353332000098-
dc.creator.orcid0000-0003-0812-4027pt_BR
dc.type.formArtigopt_BR
dc.identifier.articleide0124969pt_BR
dc.identifier.articleide0124969-
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