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

ABSTRACT: Histone lysine methylation is regulated by N?-methyltransferases, demethylases, and N?-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?-methyl lysine binding proteins are superior in accepting lysines with the d-configuration.

SUBMITTER: Belle R

PROVIDER: S-EPMC6345366 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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

Belle Roman R Al Temimi Abbas H K AHK Kumar Kiran K Pieters Bas J G E BJGE Tumber Anthony A Dunford James E JE Johansson Catrine C Oppermann Udo U Brown Tom T Schofield Christopher J CJ Hopkinson Richard J RJ Paton Robert S RS Kawamura Akane A Mecinović Jasmin J

Chemical communications (Cambridge, England) 20171201 99

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 ...[more]

PMID: 29186216

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