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Nucleic Acids Research Advance Access originally published online on March 6, 2009
Nucleic Acids Research 2009 37(8):2596-2606; doi:10.1093/nar/gkp115
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Nucleic Acids Research, 2009, Vol. 37, No. 8 2596-2606
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene Regulation, Chromatin and Epigenetics

Plasmodium falciparum heterochromatin protein 1 binds to tri-methylated histone 3 lysine 9 and is linked to mutually exclusive expression of var genes

Karla Pérez-Toledo1, Ana Paola Rojas-Meza1,2, Liliana Mancio-Silva2, Nora Adriana Hernández-Cuevas1, Dulce Maria Delgadillo1, Miguel Vargas1, Santiago Martínez-Calvillo3, Artur Scherf2 and Rosaura Hernandez-Rivas1,*

1Departamento de Biomedicina Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (IPN), Apartado Postal 14-740, 07360, México D. F., México, 2Institut Pasteur, Unité de Biologie des Interactions Hôte-Parasite – CNRS URA2581. 25, Rue du Dr. Roux, 75724 Paris, France and 3Unidad de Biomedicina, Facultad de Estudios Superiores Iztacala, Universidad Nacional Autónoma de México. Av. de los Barrios 1, Col. Los Reyes Iztacala, Tlalnepantla, Edo. de México, CP 54090, México

*To whom correspondence should be addressed. Tel: +(52) 55 5747 3325; Fax: +(52) 55 5747 3938; Email: rohernan{at}cinvestav.mx

Received December 1, 2008. Revised February 6, 2009. Accepted February 10, 2009.

Increasing experimental evidence shows a prominent role of histone modifications in the coordinated control of gene expression in the human malaria parasite Plasmodium falciparum. The search for the histone-mark-reading machinery that translates histone modifications into biological processes, such as formation of heterochromatin and antigenic variation is of foremost importance. In this work, we identified the first member of a histone modification specific recognition protein, an orthologue of heterochromatin protein 1 (PfHP1). Analysis of the PfHP1 amino-acid sequence revealed the presence of the two characteristic HP1 domains: a chromodomain (CD) and a chromo shadow domain (CSD). Recombinant CD binds to di- and tri-methylated lysine 9 from histone H3, but not to unmodified or methylated histone H3 in lysine 4. PfHP1 is able to interact with itself to form dimers, underlying its potential role in aggregating nucleosomes to form heterochromatin. Antibodies raised against PfHP1 detect this molecule in foci at the perinuclear region. ChIP analysis using anti-PfHP1 shows that this protein is linked to heterochromatin of subtelomeric non-coding repeat regions and monoallelic expression of the major virulence var gene family. This is the first report implicating an HP1 protein in the control of antigenic variation of a protozoan parasite.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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