Synthetic antagonist of a histone reader reveals and targets genes essential for inflammation

ABSTRACT: Post-translational modifications of histones determines cell lineage- or signal-specific gene expression. Depending on the type and combination of modifications, histones bind to functionally distinct effector proteins ('readers') that control gene activation or silencing. The current pharmacological modulation of the epigenome aims to control gene expression by regulation of the enzymes that catalyze post-translational histone modifications. Here we present a novel pharmacological approach that targets gene expression by interfering with the function of histone ?readers?. We describe the impact of a synthetic compound that selectively occupies the acetylated histone-binding pocket of the Bromodomain and Extra Terminal domain (BET) family of proteins and prevents their interaction with

ORGANISM(S): Mus musculus

SUBMITTER: Uwe Schaefer 

PROVIDER: E-GEOD-21910 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress