A fluorescence resonance energy transfer-based method for histone methyltransferases
Research output: Contribution to journal › Journal article › Research › peer-review
A simple dye–quencher fluorescence resonance energy transfer (FRET)-based assay for methyltransferases was developed and used to determine kinetic parameters and inhibitory activity at EHMT1 and EHMT2. Peptides mimicking the truncated histone H3 tail were functionalized in each end with a dye and a quencher, respectively. When lysine-9 residues in the peptides were methylated, they were protected from cleavage by endoproteinase–EndoLysC, whereas unmethylated peptides were cleaved, resulting in an increase in fluorescent intensity.
|Number of pages||3|
|Publication status||Published - 19 Feb 2015|
- Faculty of Health and Medical Sciences