Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.
Skip to main content

In this issue of Molecular Cell, Sampath et al. show a lysine methylase exhibits substrate promiscuity and variability in degree of product methylation (Sampath et al., 2007). Two lysines are found to be automethylated in G9a, and one is H3K9-like and can establish a docking site for HP1 chromodomain.

Original publication

DOI

10.1016/j.molcel.2007.08.002

Type

Journal article

Journal

Mol Cell

Publication Date

17/08/2007

Volume

27

Pages

521 - 522

Keywords

Animals, Epigenesis, Genetic, Histone Methyltransferases, Histone-Lysine N-Methyltransferase, Histones, Humans, Lysine, Methylation, Mice, Molecular Mimicry, Protein Methyltransferases, Signal Transduction, Substrate Specificity