Histone H1 is phosphorylated in non-replicating and infective forms of Trypanosoma cruzi

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dc.contributor.authorPorto, Rafael Marques [UNIFESP]
dc.contributor.authorAmino, Rogerio [UNIFESP]
dc.contributor.authorElias, Maria Carolina Quartim [UNIFESP]
dc.contributor.authorFaria, Marcella [UNIFESP]
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2018-06-18T11:04:08Z
dc.date.available2018-06-18T11:04:08Z
dc.date.issued2002-02-01
dc.description.abstractThe nuclear structure changes during the differentiation from growing to infective stages of Trypanosoma cruzi. As histone modifications have been correlated with structural and functional changes of chromatin, we investigated whether histones in T. cruzi are modified during the life cycle of this protozoan parasite. We found that histone H1 isolated from proliferating forms (epimastigotes) and from differentiated/infective forms (trypomastigotes) have a distinct migrating pattern in Triton-acetic acid-urea gel electrophoresis. While epimastigotes contain predominantly a fast migrating form, a slow migrating band is prominent in trypomastigotes. By metabolically labeling the cells with radioactive phosphate, we demonstrated that the slow migrating histone H 1 band is phosphorylated, and that after alkaline phosphatase treatment, it migrates as the fast form. Parasites arrested at the onset of the S phase of the cell cycle with hydroxyurea (HU) also predominantly have the phosphorylated form of histone 11:1, suggesting that phosphorylation occurs in non-replicating stages of T. cruzi. We also found that the phosphorylated histone HI is more weakly associated with the chromatin, being preferentially released at 150 mM NaCl. Therefore, histone H1 phosphorylation varies during the life cycle of T. cruzi, and might be related to changes in the chromatin structure. (C) 2002 Elsevier Science B.V. All rights reserved.en
dc.description.affiliationUNIFESP, Escola Paulista Med, Dept Microbiol Immol & Parasitol, BR-04023062 Sao Paulo, Brazil
dc.description.affiliationUnifespUNIFESP, Escola Paulista Med, Dept Microbiol Immol & Parasitol, BR-04023062 Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent265-271
dc.identifierhttp://dx.doi.org/10.1016/S0166-6851(01)00430-3
dc.identifier.citationMolecular And Biochemical Parasitology. Amsterdam: Elsevier Science Bv, v. 119, n. 2, p. 265-271, 2002.
dc.identifier.doi10.1016/S0166-6851(01)00430-3
dc.identifier.issn0166-6851
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/44920
dc.identifier.wosWOS:000173915200011
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular And Biochemical Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjecthistoneen
dc.subjectchromatinen
dc.subjectTrypanosoma cruzien
dc.titleHistone H1 is phosphorylated in non-replicating and infective forms of Trypanosoma cruzien
dc.typeinfo:eu-repo/semantics/article
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