A Nutrient-Based Cellular Model to Characterize Acetylation-Dependent Protein-Protein Interactions.

ABSTRACT: Cellular homeostasis requires the orderly expression of thousands of transcripts. Gene expression is regulated by numerous proteins that recognize post-translational modifications-in particular, the acetylation of lysine residues (Kac) on histones. In addition to affecting the general condensation state of the chromatin, acetylated histones act as anchor points for bromodomain (BRD)-containing adapter proteins. BRDs are the primary Kac reader domains in humans, and proteins containing them act as chromatin scaffolds that organize large networks of interactions to regulate transcription. To characterize BRD-dependent interaction networks, we established cell lines in which histone acetylation is dependent on acetate supplementation. To do this, we used genome editing to knock out ATP citrat

SUBMITTER: Loehr J 

PROVIDER: S-EPMC8984119 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature