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Histone methyltransferases (HMTs) play a major role in the epigenetic regulation of gene expression by catalyzing the methylation of a diverse set of histone and non-histone substrates. The observation that aberrant HMT activity plays a role in the progression of certain human malignances validates HMTs as an important new class of drug targets.
Covalent modification of DNA through methylation is catalyzed by specific DNA methyltransferases (DNMTs). DNMT1, 3a and 3b are the best characterized mammalian enzymes of this class, with DNMT1 thought to be responsible for maintenance of the methylated state, and DNMT3a and 3b responsible for de novo DNA methylation.
Several assay methods have been developed for quantifying the activity of histone deacetylases (HDACs and sirtuins), histone methyltransferases (HMTs), and histone demethylases (HDMs). These include radioactive assays, enzymelinked immunoassays (ELISA), mass spectrometry, and enzyme-coupled detection of fluorescent peptides or reaction co-products (e.g.
Post-translational modifications of histone proteins play an important part in a wide array of cellular processes including regulation of gene transcription, DNA repair, cell cycle, and metabolism control. For instance, transcriptional activation is associated with acetylation of Histone H3 on residues K9 and K14, and methylation on K4.
In eukaryotes, the covalent modification of histones has a crucial role in chromatin architecture and plays an important part in a plethora of cellular processes, from chromatin remodeling and transcriptional regulation, to DNA repair and cell cycle control. While histone acetylation is generally associated to an open chromatin state and transcriptional activation, methylation of histones has been related to either activating or repressive functions.
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