Reading and erasing of the phosphonium analogue of trimethyllysine by epigenetic proteins.

ABSTRACT: N ^ε-Methylation of lysine residues in histones plays an essential role in the regulation of eukaryotic transcription. The 'highest' methylation mark, N ^ε-trimethyllysine, is specifically recognised by N ^ε-trimethyllysine binding 'reader' domains, and undergoes demethylation, as catalysed by 2-oxoglutarate dependent JmjC oxygenases. We report studies on the recognition of the closest positively charged N ^ε-trimethyllysine analogue, i.e. its trimethylphosphonium derivative (K_Pme₃), by N ^ε-trimethyllysine histone binding proteins and N^ε-trimethyllysine demethylases. Calorimetric and computational studies with histone binding proteins reveal that H3K_P4me<

SUBMITTER: Belle R 

PROVIDER: S-EPMC7613515 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature