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

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

Autor Cunha, JPC da Google Scholar
Nakayasu, E. S. Google Scholar
Elias, M. C. Google Scholar
Pimenta, D. C. Google Scholar
Tellez-Inon, M. T. Google Scholar
Rojas, F. Google Scholar
Manuel, M. Google Scholar
Almeida, I. C. Google Scholar
Schenkman, S. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
CEPID
Consejo Nacl Invest Cient & Tecn
Univ Texas
Resumo 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.
Palavra-chave histone H1
phosphorylation
cell cycle
Trypanosoma cruzi
phosphatase
CDK
Idioma Inglês
Data de publicação 2005-03-01
Publicado em Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 140, n. 1, p. 75-86, 2005.
ISSN 0166-6851 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 75-86
Fonte http://dx.doi.org/10.1016/j.molbiopara.2004.12.007
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000227271200008
Endereço permanente http://repositorio.unifesp.br/handle/11600/28183

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