Molecular basis for substrate recognition by lysine methyltransferases and demethylases

• Published in: Biochimica et biophysica acta Vol. 1839; no. 12; pp. 1404 - 1415
• Main Authors: Del Rizzo, Paul A., Trievel, Raymond C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2014
• Subjects: Animals; Chromatin; Histone Demethylases - chemistry; Histone Demethylases - genetics; Histone Demethylases - metabolism; Histone lysine methylation; Histone-Lysine N-Methyltransferase - chemistry; Histone-Lysine N-Methyltransferase - genetics; Histone-Lysine N-Methyltransferase - metabolism; Histone-Lysine N-Methyltransferase - physiology; Histones - chemistry; Histones - metabolism; Humans; Lysine - chemistry; Lysine - metabolism; Lysine demethylase; Lysine methyltransferase; Methylation; Models, Molecular; Protein Binding - genetics; Substrate Specificity; Transcription; Histone lysine methylation; Chromatin; Lysine methyltransferase; Transcription; Lysine demethylase; Substrate specificity

Lysine methylation has emerged as a prominent covalent modification in histones and non-histone proteins. This modification has been implicated in numerous genomic processes, including heterochromatinization, cell cycle progression, DNA damage response, DNA replication, genome stability, and epigene...