Unknown

Dataset Information

0

Live-cell studies of p300/CBP histone acetyltransferase activity and inhibition.

ABSTRACT: 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.

SUBMITTER: Dancy BM 

PROVIDER: S-EPMC3517098 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Live-cell studies of p300/CBP histone acetyltransferase activity and inhibition.

Dancy Beverley M BM   Crump Nicholas T NT   Peterson Daniel J DJ   Mukherjee Chandrani C   Bowers Erin M EM   Ahn Young-Hoon YH   Yoshida Minoru M   Zhang Jin J   Mahadevan Louis C LC   Meyers David J DJ   Boeke Jef D JD   Cole Philip A PA  

Chembiochem : a European journal of chemical biology 20120907 14

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  ...[more]

Similar Datasets

Unknown Analysis of p300/CBP histone acetyltransferase regulation using circular permutation and semisynthesis.
| S-EPMC2811879 | biostudies-literature
Unknown Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.
| S-EPMC2574607 | biostudies-literature
Unknown Probing the reaction coordinate of the p300/CBP histone acetyltransferase with bisubstrate analogs.
| S-EPMC3076313 | biostudies-literature
Unknown The SV40 T antigen modulates CBP histone acetyltransferase activity.
| S-EPMC162251 | biostudies-literature
Unknown Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function.
| S-EPMC2643075 | biostudies-literature
Unknown ELF3 modulates type II collagen gene (COL2A1) transcription in chondrocytes by inhibiting SOX9-CBP/p300-driven histone acetyltransferase activity.
| S-EPMC5326708 | biostudies-other
Unknown Plant orthologs of p300/CBP: conservation of a core domain in metazoan p300/CBP acetyltransferase-related proteins.
| S-EPMC30400 | biostudies-literature
Unknown Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor.
| S-EPMC2884008 | biostudies-literature
Unknown MOF as an evolutionarily conserved histone crotonyltransferase and transcriptional activation by histone acetyltransferase-deficient and crotonyltransferase-competent CBP/p300.
| S-EPMC5441097 | biostudies-literature
Unknown Histone Acetyltransferase (HAT) P300/CBP Inhibitors Induce Synthetic Lethality in PTEN-Deficient Colorectal Cancer Cells through Destabilizing AKT.
| S-EPMC7211175 | biostudies-literature