Developmental regulation of N-terminal H2B methylation in Drosophila melanogaster

Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, 80336 Munich, Germany.
Nucleic Acids Research (Impact Factor: 9.11). 11/2011; 40(4):1536-49. DOI: 10.1093/nar/gkr935
Source: PubMed

ABSTRACT Histone post-translational modifications play an important role in regulating chromatin structure and gene expression in vivo. Extensive studies investigated the post-translational modifications of the core histones H3 and H4 or the linker histone H1. Much less is known on the regulation of H2A and H2B modifications. Here, we show that a major modification of H2B in Drosophila melanogaster is the methylation of the N-terminal proline, which increases during fly development. Experiments performed in cultured cells revealed higher levels of H2B methylation when cells are dense, regardless of their cell cycle distribution. We identified dNTMT (CG1675) as the enzyme responsible for H2B methylation. We also found that the level of N-terminal methylation is regulated by dART8, an arginine methyltransferase that physically interacts with dNTMT and asymmetrically methylates H3R2. Our results demonstrate the existence of a complex containing two methyltransferases enzymes, which negatively influence each other's activity.

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Available from: Ignasi Forne, Sep 27, 2015
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    • "NRMT was shown to be promiscuous and is able to methylate protein substrates other than RCC1, such as SET (also known as TAF-I or PHAPII) and the retinoblastoma protein RB [8]. An ortholog of NRMT in Drosophila melanogaster , dNTMT, was shown to catalyze methylation of histone H2B [10]. For bacteria, methylation of the ribosomal protein L11 has been relatively well characterized. "
    Dataset: FEBS CypM
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