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Review
. 2013 May;8(5):457-63.
doi: 10.4161/epi.24451. Epub 2013 Apr 27.

On your histone mark, SET, methylate!

Olivier Binda  1
Affiliations
Review

On your histone mark, SET, methylate!

Olivier Binda. Epigenetics. 2013 May.

Abstract

Lysine methylation of histones and non-histone proteins has emerged in recent years as a posttranslational modification with wide-ranging cellular implications beyond epigenetic regulation. The molecular interactions between lysine methyltransferases and their substrates appear to be regulated by posttranslational modifications surrounding the lysine methyl acceptor. Two very interesting examples of this cross-talk between methyl-lysine sites are found in the SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain-containing lysine methyltransferases SET7 and SETDB1, whereby the histone H3 trimethylated on lysine 4 (H3K4 (me3) ) modification prevents methylation by SETDB1 on H3 lysine 9 (H3K9) and the histone H3 trimethylated on lysine 9 (H3K9 (me3) ) modification prevents methylation by SET7 on H3K4. A similar cross-talk between posttranslational modifications regulates the functions of non-histone proteins such as the tumor suppressor p53 and the DNA methyltransferase DNMT1. Herein, in cis effects of acetylation, phosphorylation, as well as arginine and lysine methylation on lysine methylation events will be discussed.

Keywords: chromatin; chromatin signaling; lysine methylation; lysine methyltransferase.

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Figures

None
Figure 1. Cross-talk on histone H3 N-terminus.The amino acid sequence of the histone tail of H3 is annotated to highlight the position of key modified residues. Black lines represents published cross-talk events. White lines represent putative cross-talk events. The dashed black line between H3R2 and H3K4 represents the antagonistic cross-talk between H3R2me2a and H3K4me3. The purple arrows between H3R2 and H3K4 highlight the permissive cross-talk between H3R2me2s and H3K4me3.
See this image and copyright information in PMC

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