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Lysine methyltransferases are enyzmes that catalyze the transfer of methyl groups from S-adenosylmethionine (SAM) to the lysine residues on histones, particularly histones H3 and H4. The dysregulation of this methylation is critical in the development of cancer.
Lysine methyltransferases, or KMTs, are enzymes that catalyze the transfer of methyl groups from S-adenosylmethionine (SAM) to the lysine residues on histones. Upward of 24 human protein lysine methyltransferases have been described and they belong to the histone methyltransferase group of enzymes, which also includes protein arginine methyltransferases. They are also closely related in biological activity to the DNA methyltransferases.
Histones represent the major protein component of chromatin, around which DNA is coiled within the nucleus. Modification of histone protein by methylation induces chromatin remodeling which in turn alters gene expression. Histone methylation is an integral epigenetic process during development and represents an important mechanism of transcriptional regulation and chromatin remodeling. Dysregulation of histone methylation has been implicated in diseases including cancer.
Histone methylation by KMTs occurs predominantly on lysine residues in histones H3 and H4, and multiple methyl groups may be added to each residue.The epigenetic effects of histone methylation are dependent on the residue undergoing methylation and the degree of methylation. Consequently different types of lysine methylation are associated with different functions in the regulation of gene expression. Lysine methylation can induce both transcriptional activation and silencing.
Tocris offers the following scientific literature for Lysine Methyltransferases to showcase our products. We invite you to request* your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
Written by Susanne Müller-Knapp and Peter J. Brown, this review gives an overview of the development of chemical probes for epigenetic targets, as well as the impact of these tool compounds being made available to the scientific community. In addition, their biological effects are also discussed. Epigenetic compounds available from Tocris are listed.
Produced by Tocris and updated in 2014, the epigenetics research bulletin gives an introduction into mechanisms of epigenetic regulation, and highlights key Tocris products for epigenetics targets including:
This poster summarizes the main epigenetic targets in cancer. The dysregulation of epigenetic modifications has been shown to result in oncogenesis and cancer progression. Unlike genetic mutations, epigenetic alterations are considered to be reversible and thus make promising therapeutic targets.
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|
|Euchromatic histone-lysine N-methyltransferase 1 (GLP)||Human||EHMT1||NM_024757||Q9H9B1|
|Euchromatic histone-lysine N-methyltransferase 2 (G9a)||Human||EHMT2||NM_006709||Q96KQ7|
|SET domain containing 2||Human||SETD2||NM_014159||Q9BYW2|
|SET domain containing (lysine methyltransferase) 7 (SET9)||Human||SETD7||NM_030648||Q8WTS6|
|SET domain containing (lysine methyltransferase) 8||Human||SETD8||NM_020382||Q9NQR1|
|SET domain, bifurcated 1||Human||SETDB1||NM_001145415||Q15047|
|SET domain, bifurcated 2||Human||SETDB2||NM_031915||Q96T68|
|SET domain containing 1A||Human||SETD1A||NM_014712||O15047|
|SET domain containing 1B||Human||SETD1B||XM_037523||Q9UPS6|
|Nuclear receptor binding SET protein domain 1||Human||NSD1||NM_172349||Q96L73|
|SET and MYND domain containing 2||Human||SMYD2||NM_020197||Q9NRG4|
|PR domain containing 2m with ZNF domain||Human||PRDM2||NM_012231||Q13029|