Histone Methyltransferases

Histones are methylated at many lysine and arginine residues. Extra complexity of these modifications arise from the fact that this modification may be one of the three different forms such as mono-, di- and tri-methyl for lysine and mono- or di-methyl symmetrical or asymmetrical form for arginine residues. The enzymes that mediate these modifications using S-adenosyl-L-methionine are a class of SET domain containing proteins known as histone methyltransferases (1, 2). Inhibitors for various histone methyltransferases are attractive for pharmaceutical therapeutics (3). A recently developed technique uses fluorescent immunodetection of adenosine monophosphate (AMP), which is formed from the reaction product S-adenosylhomocysteine in a dual-enzyme coupling step (4). This novel method allows for high-throughput screening.


  1. Greer E.L. and Shi, Y. (2012) Nat Rev Genet. Apr 3; 13(5):343-57. PMID: 22473383
  2. DiLorenzo A. and Bedford, M.T. (2011) FEBS Lett. Jul 7; 585(13):2024-31. PMID: 21074527
  3. Arrowsmith CH et al. (2012) Nat Rev Drug Discov. Apr 13; 11(5): 384-400. PMID: 22498752
  4. Tony A. Klink (2012) Journal of Biomolecular Screening. 17(1): 59-70. PMID: 21956169

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