Projects per year
Histone methyltransferases (HMTs) catalyze the methylation of lysine and arginine residues in histone as well as nonhistone substrates. In vitro histone methyltransferase assays have been instrumental in identifying HMTs, and they continue to be invaluable tools for the study of these important enzymes, revealing novel substrates and modes of regulation.Here we describe a universal protocol to examine HMT activity in vitro that can be adapted to a range of HMTs, substrates, and experimental objectives. We provide protocols for the detection of activity based on incorporation of 3H-labeled methyl groups from S-adenosylmethionine (SAM), methylation-specific antibodies, and quantification of the reaction product S-adenosylhomocysteine (SAH).
|Title of host publication||Histone methyltransferases|
|Subtitle of host publication||Methods and protocols|
|Number of pages||19|
|Publication status||E-pub ahead of print - 23 Jun 2022|
|Name||Methods in molecular biology (Clifton, N.J.)|
- histone methyltransferases
- histone-lysine N-methyltransferase
- protein processing
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- 3 Finished
1/06/15 → 31/05/22
Roles of symmetric and asymmetric histone H3 lysine 27 trimethylation in gene repression and epigenetic inheritance
Voigt, P. & Finnegan, D.
1/11/14 → 31/12/21