Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle

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dc.contributor.author Cunha, JPC da
dc.contributor.author Nakayasu, E. S.
dc.contributor.author Elias, M. C.
dc.contributor.author Pimenta, D. C.
dc.contributor.author Tellez-Inon, M. T.
dc.contributor.author Rojas, F.
dc.contributor.author Manuel, M.
dc.contributor.author Almeida, I. C.
dc.contributor.author Schenkman, S.
dc.date.accessioned 2016-01-24T12:37:43Z
dc.date.available 2016-01-24T12:37:43Z
dc.date.issued 2005-03-01
dc.identifier http://dx.doi.org/10.1016/j.molbiopara.2004.12.007
dc.identifier.citation Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 140, n. 1, p. 75-86, 2005.
dc.identifier.issn 0166-6851
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/28183
dc.description.abstract Histone H1 of most eukaryotes is phosphorylated during the cell cycle progression and seems to play a role in the regulation of chromatin structure, affecting replication and chromosome condensation. in trypanosomatids, histone HI lacks the globular domain and is shorter when compared with the histone of other eukaryotes. We have previously shown that in Topanosoma cruzi, the agent of Chagas' disease, histone H1 is phosphorylated and this increases its dissociation from chromatin. Here, we demonstrate using mass spectrometry analysis that T. cruzi histone H1 is only phosphorylated at the serine 12 in the sequence SPKK, a typical cyclin-dependent kinase site. We also found a correlation between the phosphorylation state of histone H1 and the cell cycle. Hydroxyurea and lactacystin, which, respectively, arrest parasites at the G1/S and G2/M stages of the cell cycle, increased the level of histone HI phosphorylation. Cyclin-dependent kinase-related enzymes TzCRK3, and less intensely the TzCRK1 were able to phosphorylate histone H1w in vitro. Histone H1 dephosphorylation was prevented by treating the parasites with okadaic acid but not with calyculin A. These findings suggest that T. cruzi histone H1 phosphorylation is promoted by cyclin dependent kinases, present during S through G2 phase of the cell cycle, and its dephosphorylation is promoted by specific phosphatases. (C) 2004 Elsevier B.V. All rights reserved. en
dc.format.extent 75-86
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Molecular and Biochemical Parasitology
dc.rights Acesso restrito
dc.subject histone H1 en
dc.subject phosphorylation en
dc.subject cell cycle en
dc.subject Trypanosoma cruzi en
dc.subject phosphatase en
dc.subject CDK en
dc.title Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution CEPID
dc.contributor.institution Consejo Nacl Invest Cient & Tecn
dc.contributor.institution Univ Texas
dc.description.affiliation Universidade Federal de São Paulo, EPM, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliation USP, ICB, Dept Parasitol, BR-09500900 São Paulo, Brazil
dc.description.affiliation CEPID, Inst Butantan, CAT, Ctr Toxicol Aplicada, São Paulo, Brazil
dc.description.affiliation Consejo Nacl Invest Cient & Tecn, INGEBI, Inst Invest Ingn Genet & Biol Mol, RA-1428 Buenos Aires, DF, Argentina
dc.description.affiliation Univ Texas, Dept Biol Sci, El Paso, TX 79968 USA
dc.description.affiliationUnifesp Universidade Federal de São Paulo, EPM, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.identifier.doi 10.1016/j.molbiopara.2004.12.007
dc.description.source Web of Science
dc.identifier.wos WOS:000227271200008



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