4.1 Article

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

Journal

MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 172, Issue 2, Pages 141-144

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2010.03.013

Keywords

Trypanosoma brucei; Histone modification; Transcription regulation; Chromatin immunoprecipitation; High-throughput DNA sequencing

Funding

  1. Boehringer Ingelheim Fonds
  2. David Rockefeller Graduate Program
  3. National Institute of Allergy and Infectious Diseases (NIAID) of the U.S. National Institutes of Health (NIH) [R01AI021729]

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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. (C) 2010 Elsevier B.V. All rights reserved.

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