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Cells 2018, 7(3), 17; https://doi.org/10.3390/cells7030017

Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin

Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Pauwelsstrasse 30, 52057 Aachen, Germany
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Received: 18 January 2018 / Revised: 22 February 2018 / Accepted: 27 February 2018 / Published: 2 March 2018
(This article belongs to the Section Cell Nuclei: Function, Transport and Receptors)
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Abstract

Regulation of gene expression is achieved by sequence-specific transcriptional regulators, which convey the information that is contained in the sequence of DNA into RNA polymerase activity. This is achieved by the recruitment of transcriptional co-factors. One of the consequences of co-factor recruitment is the control of specific properties of nucleosomes, the basic units of chromatin, and their protein components, the core histones. The main principles are to regulate the position and the characteristics of nucleosomes. The latter includes modulating the composition of core histones and their variants that are integrated into nucleosomes, and the post-translational modification of these histones referred to as histone marks. One of these marks is the methylation of lysine 4 of the core histone H3 (H3K4). While mono-methylation of H3K4 (H3K4me1) is located preferentially at active enhancers, tri-methylation (H3K4me3) is a mark found at open and potentially active promoters. Thus, H3K4 methylation is typically associated with gene transcription. The class 2 lysine methyltransferases (KMTs) are the main enzymes that methylate H3K4. KMT2 enzymes function in complexes that contain a necessary core complex composed of WDR5, RBBP5, ASH2L, and DPY30, the so-called WRAD complex. Here we discuss recent findings that try to elucidate the important question of how KMT2 complexes are recruited to specific sites on chromatin. This is embedded into short overviews of the biological functions of KMT2 complexes and the consequences of H3K4 methylation. View Full-Text
Keywords: ASH2L; chromatin; core histone; DPY30; gene expression; histone mark; histone modification; KMT2; mixed-lineage leukemia; methylation; MLL; post-translational modification; RBBP5; transcription; WDR5 ASH2L; chromatin; core histone; DPY30; gene expression; histone mark; histone modification; KMT2; mixed-lineage leukemia; methylation; MLL; post-translational modification; RBBP5; transcription; WDR5
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Bochyńska, A.; Lüscher-Firzlaff, J.; Lüscher, B. Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin. Cells 2018, 7, 17.

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