ePrints

On your histone mark, SET, methylate!

Lookup NU author(s): Dr Olivier Binda

Downloads

• Published version [.pdf]

Abstract

Lysine methylation of histones and non-histone proteins has emerged in recent years as a post-translational modification with wide-ranging cellular implications beyond epigenetic regulation. The molecular interactions between lysine methyltransferases and their substrates appear to be regulated by post-translational 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 (H3K4me3) modification prevents methylation by SETDB1 on H3 lysine 9 (H3K9) and the histone H3 trimethylated on lysine 9 (H3K9me3) modification prevents methylation by SET7 on H3K4. A similar cross-talk between post-translational modifications regulates the functions of non-histone proteins such as the tumour 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.

Publication metadata

Author(s): Binda O

Publication type: Article

Publication status: Published

Journal: Epigenetics

Year: 2013

Volume: 8

Issue: 5

Pages: 457-463

Print publication date: 27/04/2013

Date deposited: 03/07/2013

ISSN (print): 1559-2294

ISSN (electronic): 1559-2308

Publisher: Landes Bioscience

URL: http://dx.doi.org/10.4161/epi.24451

DOI: 10.4161/epi.24451

Altmetrics

Share