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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.

Original publication

DOI

10.1039/c7cc08028j

Type

Journal article

Journal

Chemical communications (Cambridge, England)

Publication Date

12/2017

Volume

53

Pages

13264 - 13267

Addresses

Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. j.mecinovic@science.ru.nl.

Keywords

Methyltransferases, Lysine, Epigenesis, Genetic, Molecular Conformation, Methylation, Stereoisomerism, Thermodynamics, Models, Molecular, Biocatalysis, Histone Demethylases