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

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...

全面介绍

书目详细资料
Main Authors: Belle, R, Al Temimi, A, Kumar, K, Pieters, B, Tumber, A, Dunford, J, Johansson, C, Oppermann, U, Brown, T, Schofield, C, Hopkinson, R, Paton, R, Kawamura, A, Mecinović, J
格式: Journal article
语言:English
出版: Royal Society of Chemistry 2017
实物特征
总结: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.