Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.

ABSTRACT: Protein lysine methylation is a distinct class of post-translational modifications because it minimally alters the size and positive charge of the lysine side chain. In cellular contexts, the human genome encodes over 60 protein lysine methyltransferases (PKMTs), with the S-adenosyl-l-methionine (SAM) cofactor as the methyl donor, to modify thousands of lysine sites on histones and nonhistone targets in a highly orchestrated manner. The biological roles of protein lysine methylation are increasingly implicated in epigenetic regulation to define diverse cell fates, and their dysregulation is frequently associated with developmental abnormalities and various aspects of cancerous malignancy. However, it has been challenging to annotate the multiple upstream methyltransferase(s) in para

SUBMITTER: Zong Y 

PROVIDER: S-EPMC12921865 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature