ePrints

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

Lookup NU author(s): Professor Akane Kawamura

Downloads

• Accepted version [.pdf]

Licence

This is the authors' accepted manuscript of an article that has been published in its final definitive form by Royal Society of Chemistry, 2017.

For re-use rights please refer to the publisher's terms and conditions.

Abstract

© 2017 The Royal Society of Chemistry. Histone lysine methylation is regulated by N ϵ -methyltransferases, demethylases, and N ϵ -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, N ϵ -methyl lysine binding proteins are superior in accepting lysines with the d-configuration.

Publication metadata

Author(s): Belle R, Al Temimi AHK, Kumar K, Pieters BJGE, Tumber A, Dunford JE, Johansson C, Oppermann U, Brown T, Schofield CJ, Hopkinson RJ, Paton RS, Kawamura A, Mecinovic J

Publication type: Article

Publication status: Published

Journal: Chemical Communications

Year: 2017

Volume: 53

Issue: 99

Pages: 13264-13267

Print publication date: 25/12/2017

Online publication date: 23/11/2017

Acceptance date: 23/11/2017

Date deposited: 14/10/2019

ISSN (print): 1359-7345

ISSN (electronic): 1364-548X

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/c7cc08028j

DOI: 10.1039/c7cc08028j

PubMed id: 29186216

Altmetrics

Share