Eukaryotic Cell
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EC Accepts, published online ahead of print on 15 February 2008
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Eukaryotic Cell doi:10.1128/EC.00460-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Histone H1 of Trypanosoma cruzi is concentrated in the nucleolus region and disperses upon phosphorylation during progression to mitosis

Luciana M. Gutiyama, Julia P. Chagas da Cunha, and Sergio Schenkman*

Departamento de Microbiologia, Imunologia e Parasitologia, Universidade Federal de São Paulo, Rua Botucatu 862 8ª, 04023-062 São Paulo, S.P., Brazil

* To whom correspondence should be addressed. Email: sschenkman{at}unifesp.br.


  Abstract

Phosphorylation of histone H1 is intimately related to the cell cycle progression in higher eukaryotes, reaching maximum levels during mitosis. We have previously shown that in the flagellated protozoan Trypanosoma cruzi, which does not condense chromatin during mitosis, histone H1 is phosphorylated at a single cyclin dependent kinase site. By using an antibody that recognizes specifically the phosphorylated T. cruzi histone H1 site, we now confirmed that T. cruzi histone H1 is also phosphorylated in a cell cycle dependent manner. Differently from core histones, in G1 and S phases of the cell cycle, the bulk of non-phosphorylated histone H1 is concentrated in the central regions of the nucleus, which contains the nucleolus and less densely packed chromatin. When cells pass G2, histone H1 becomes phosphorylated and starts to diffuse. On the onset of mitosis, the histone H1 phosphorylation is maximal and found in the entire nuclear space. As permeabilized parasites loose preferentially the phosphorylated histone H1, we conclude that this modification promotes its release from less condensed and nucleolar chromatin after G2.






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