Trypanosoma cruzi bromodomain factor 2 (BDF2) binds to acetylated histones and is accumulated after UV irradiation

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dc.contributor.authorVanina Villanova, Gabriela
dc.contributor.authorNardelli, Sheila Cristina [UNIFESP]
dc.contributor.authorCribb, Pamela
dc.contributor.authorMagdaleno, Anahi [UNIFESP]
dc.contributor.authorSilber, Ariel Mariano [UNIFESP]
dc.contributor.authorMotta, Maria Cristina M.
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.contributor.authorSerra, Esteban
dc.contributor.institutionInst Mol & Cellular Biol
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.date.accessioned2016-01-24T13:52:30Z
dc.date.available2016-01-24T13:52:30Z
dc.date.issued2009-05-01
dc.description.abstractHistone tail post-translational modifications (acetylation, methylation, phosphorylation, ubiquitination and ADP-ribosylation) regulate many cellular processes. Among these modifications, phosphorylation, methylation and acetylation have already been described in trypanosomatid histones. Bromodomains, together with chromodomains and histone-binding SANT domains, were proposed to be responsible for histone code reading. the Trypanosoma cruzi genome encodes four coding sequences (CDSs) that contain a bromodomain, named TcBDF1-4. Here we show that one of those, TcBDF2, is expressed in discrete regions inside the nucleus of all the parasite life cycle stages and binds H4 and H2A purified histones from T. cruzi. Immunolocalization experiments using both anti-histone H4 acetylated peptides and anti-TcBDF2 antibodies determined that TcBDF2 co-localizes with histone H4 acetylated at lysines K10 and K14. TcDBF2 and K10 acetylated H4 interaction was confirmed by co-immunoprecipitation. It is also shown that TcBDF2 was accumulated after UV irradiation of T. cruzi epimastigotes. These results suggest that TcBDF2 could be taking part in a chromatin remodelling complex in T. cruzi. (C) 2009 Australian Society for Parasitology Inc. Published by Elsevier B.V. All rights reserved.en
dc.description.affiliationInst Mol & Cellular Biol, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Santa Fe, Argentina
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv Fed Rio de Janeiro, Inst Biofis Carlos Chagas Filho, BR-21949900 Rio de Janeiro, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-04023062 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipNational Research Council (CONICET), Argentina
dc.description.sponsorshipANPCyT
dc.description.sponsorshipCONICET
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent665-673
dc.identifierhttp://dx.doi.org/10.1016/j.ijpara.2008.11.013
dc.identifier.citationInternational Journal for Parasitology. Oxford: Elsevier B.V., v. 39, n. 6, p. 665-673, 2009.
dc.identifier.doi10.1016/j.ijpara.2008.11.013
dc.identifier.issn0020-7519
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/31497
dc.identifier.wosWOS:000264962200004
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInternational Journal for Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTrypanosomesen
dc.subjectBromodomainen
dc.subjectTcBDF2en
dc.subjectHistone H4en
dc.titleTrypanosoma cruzi bromodomain factor 2 (BDF2) binds to acetylated histones and is accumulated after UV irradiationen
dc.typeinfo:eu-repo/semantics/article
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