7 research outputs found
Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins
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190207.pdf (preprint version ) (Open Access
Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition
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- 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
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- 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