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Histone acetyltransferase enzymes (HATs) are important therapeutic targets, but there are few cell-based assays available for evaluating the pharmacodynamics of HAT inhibitors. Here we present the application of a FRET-based reporter, Histac, in live-cell studies of p300/CBP HAT inhibition, by both genetic and pharmacologic disruption. shRNA knockdown of p300/CBP led to increased Histac FRET, thus suggesting a role for p300/CBP in the acetylation of the histone H4 tail. Additionally, we describe a new p300/CBP HAT inhibitor, C107, and show that it can also increase cellular Histac FRET. Taken together, these studies provide a live-cell strategy for identifying and evaluating p300/CBP inhibitors.

Original publication

DOI

10.1002/cbic.201200381

Type

Journal article

Journal

Chembiochem

Publication Date

24/09/2012

Volume

13

Pages

2113 - 2121

Keywords

Acetylation, Animals, COS Cells, Cell Survival, Chlorocebus aethiops, Enzyme Inhibitors, Fluorescence Resonance Energy Transfer, RNA Interference, RNA, Small Interfering, Recombinant Proteins, p300-CBP Transcription Factors