Histone Methyltransferase in Human Cancer

Abstract

Histone lysine and arginine residues are related to post-translational modifications including methylation, phosphorylation, acetylation, ubiquitination, and sumoylation. The combination these modifications regulates critical DNA processes including replication, repair, and transcription. The size and function of eukaryotic genomes require that specific mechanisms for the stability of DNA. Such mechanism is the comprise of DNA with histones to form chromatin which helps in gene expression. The most important thins is that histones impact transcriptional activity is through site-specific enzymatic modification of the amino terminal histone “tails”, which can alter the spectrum of chromatin-associated proteins and hence transcriptional states. Among the well known modifications of histones, lysine methylation is the best one to represent a relatively stable mark which might be suitable for stable activation or repression, depending upon the site modified., The activity of enzymes that modify histone lysine and arginine residues have been correlated with a variety of human diseases like arthritis, cancer, heart disease, diabetes, and neurological disorders. Thus, this is important to understand the total kinetic and chemical mechanisms of these enzymes. Many HMTs have been linked to different types of cancer; however, in many cases we only have limited knowledge regarding the molecular mechanisms by which the HMTs contribute to disease development.