Eukaryotic Cell
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Other Versions of this Article:
EC.00460-07v1
7/4/560    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Gutiyama, L. M.
Right arrow Articles by Schenkman, S.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gutiyama, L. M.
Right arrow Articles by Schenkman, S.
Eukaryotic Cell, April 2008, p. 560-568, Vol. 7, No. 4
1535-9778/08/$08.00+0     doi:10.1128/EC.00460-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Histone H1 of Trypanosoma cruzi Is Concentrated in the Nucleolus Region and Disperses upon Phosphorylation during Progression to Mitosis{triangledown} ,{dagger}

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

Received 22 December 2007/ Accepted 5 February 2008

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 have now confirmed that T. cruzi histone H1 is also phosphorylated in a cell cycle-dependent manner. Differently from core histones, the bulk of nonphosphorylated histone H1 in G1 and S phases of the cell cycle 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. At the onset of mitosis, histone H1 phosphorylation is maximal and found in the entire nuclear space. As permeabilized parasites preferentially lose phosphorylated histone H1, we conclude that this modification promotes its release from less condensed and nucleolar chromatin after G2.

* Corresponding author. Mailing address: Departamento de Microbiologia, Imunologia e Parasitologia, Universidade Federal de São Paulo, Rua Botucatu 862 8A, 04023-062 São Paulo, S.P., Brazil. Phone: 55 11 55764551. Fax: 55 11 55715877. E-mail: sschenkman{at}unifesp.br

{triangledown} Published ahead of print on 15 February 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, April 2008, p. 560-568, Vol. 7, No. 4
1535-9778/08/$08.00+0     doi:10.1128/EC.00460-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Appl. Environ. Microbiol. Infect. Immun. J. Bacteriol.
Mol. Cell Biol. Microbiol. Mol. Biol. Rev. ALL ASM JOURNALS
Copyright © 2008 by the American Society for Microbiology.