Issue 99, 2017

Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition

Abstract

Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing L- and D-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the D-configuration.

Graphical abstract: Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition

Supplementary files

Article information

Article type
Communication
Submitted
17 Oct 2017
Accepted
23 Nov 2017
First published
23 Nov 2017

Chem. Commun., 2017,53, 13264-13267

Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition

R. Belle, A. H. K. Al Temimi, K. Kumar, B. J. G. E. Pieters, A. Tumber, J. E. Dunford, C. Johansson, U. Oppermann, T. Brown, C. J. Schofield, R. J. Hopkinson, R. S. Paton, A. Kawamura and J. Mecinović, Chem. Commun., 2017, 53, 13264 DOI: 10.1039/C7CC08028J

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