A fluorescence resonance energy transfer-based method for histone methyltransferases
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A fluorescence resonance energy transfer-based method for histone methyltransferases. / Devkota, Kanchan; Lohse, Brian; Nyby Jakobsen, Camilla; Berthelsen, Jens; Clausen, Rasmus Prætorius.
In: Analytical Biochemistry, Vol. 476, 19.02.2015, p. 78-80.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A fluorescence resonance energy transfer-based method for histone methyltransferases
AU - Devkota, Kanchan
AU - Lohse, Brian
AU - Nyby Jakobsen, Camilla
AU - Berthelsen, Jens
AU - Clausen, Rasmus Prætorius
PY - 2015/2/19
Y1 - 2015/2/19
N2 - 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.
AB - 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.
KW - Faculty of Health and Medical Sciences
U2 - 10.1016/j.ab.2015.02.012
DO - 10.1016/j.ab.2015.02.012
M3 - Journal article
C2 - 25703602
VL - 476
SP - 78
EP - 80
JO - Analytical Biochemistry
JF - Analytical Biochemistry
SN - 0003-2697
ER -
ID: 135502040