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Histone H3 trimethylated at lysine 4 is enriched at probable transcription start sites in Trypanosoma brucei

https://doi.org/10.1016/j.molbiopara.2010.03.013Get rights and content

Abstract

Recent studies have identified histone modifications and suggested a role for epigenetic gene regulation in Trypanosoma brucei. The histone modification H4K10ac and histone variants H2AZ and H2BV localize to probable sites of transcription initiation. Although all T. brucei histones have very evolutionarily divergent N-terminal tails, histone H3 shows conservation with other eukaryotic organisms in 6 of 8 amino acids encompassing lysine 4. Tri-methylation of H3K4 is generally associated with transcription. We therefore generated a specific antibody to T. brucei H3K4me3 and performed chromosome immunoprecipitation and high-throughput sequencing. We show that H3K4me3 is enriched at the start of polycistronic transcription units at divergent strand-switch regions and at other sites of RNA polymerase II transcription reinitiation. H3K4me3 largely co-localizes with H4K10ac, but with a skew towards the upstream side of the H4K10ac peak, suggesting that it is a component of specific nucleosomes that play a role in Pol II transcription initiation.

Graphical abstract

The histone modification H3K4me3 is enriched at probable sites of transcription initiation in Trypanosoma brucei and co-localizes with H4K10ac and histone variants H2AZ and H2Bv.

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Acknowledgements

This work was supported by fellowships from Boehringer Ingelheim Fonds and the David Rockefeller Graduate Program [TNS] and by Grant No. R01AI021729 from the National Institute of Allergy and Infectious Diseases (NIAID) of the U.S. National Institutes of Health (NIH). The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIAID or the NIH.

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    Present address: Unité de Biologie des Interactions Hôte-Parasite, CNRS URA2581, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris, France.

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