Substrate and product specificities of SET domain methyltransferases

• Published in: Epigenetics Vol. 6; no. 9; pp. 1059 - 1067
• Main Authors: Del Rizzo, Paul A., Trievel, Raymond C.
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01.09.2011; Landes Bioscience
• Subjects: Binding; Biology; Bioscience; Calcium; Cancer; Catalytic Domain; Cell; Cycle; Enzyme Activation; Histone-Lysine N-Methyltransferase - chemistry; Histones - chemistry; Humans; Landes; Lysine - chemistry; Methylation; Myeloid-Lymphoid Leukemia Protein - chemistry; NF-kappa B - chemistry; Organogenesis; Point-of-View; Protein Interaction Mapping; Protein Structure, Tertiary; Proteins; Structure-Activity Relationship; Substrate Specificity

SET domain lysine methyltransferases (KMTs) catalyze the site- and state-specific methylation of lysine residues in histone and non-histone substrates. These modifications play fundamental roles in transcriptional regulation, heterochromatin formation, X chromosome inactivation and DNA damage respon...