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...

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Bibliographic Details
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
Format: Journal article
Language:English
Published: Royal Society of Chemistry 2017
Description
Summary: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.