Reference - Detail
|Author||Dancy BM, Crump NT, Peterson DJ, Mukherjee C, Bowers EM, Ahn YH, Yoshida M, Zhang J, Mahadevan LC, Meyers DJ, Boeke JD, Cole PA.|
|Title||Live-cell studies of p300/CBP histone acetyltransferase activity and inhibition.|
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.
|MeSH||Acetylation Animals COS Cells Cell Survival / drug effects Cercopithecus aethiops Enzyme Inhibitors / chemical synthesis Enzyme Inhibitors / chemistry Enzyme Inhibitors / pharmacology Fluorescence Resonance Energy Transfer RNA Interference RNA, Small Interfering / metabolism Recombinant Proteins / antagonists & inhibitors Recombinant Proteins / genetics Recombinant Proteins / metabolism p300-CBP Transcription Factors / antagonists & inhibitors* p300-CBP Transcription Factors / genetics p300-CBP Transcription Factors / metabolism|
|DNA material||Histac pcDNA3.1 (RDB12840)|