Work

Site-specific azide-acetyllysine photochemistry on epigenetic readers for interactome profiling

Year: 2017

Type: article

Abstract: AzF) without compromising its ability to recognize acetylated lysine residues in histone proteins. We establish the binding efficiency, substrate specificity and crosslinking ability of the engineered 'reader' module in biochemical assays. Applying IBPP, we uncovered novel acetylated interacting partners of BRD4, such as transcription factors, expanding on its previously unappreciated role in diverse biological processes. By setting up an azide-acetyllysine photoreaction deep inside the bromodomain aromatic cage as a means to detect protein acetylation, our approach provides a potentially general platform for rapid and unbiased profiling of interacting partners of diverse epigenetic readers whose functions in eukaryotic gene regulation remain convoluted.

Source: Chemical Science

DOI: 10.1039/c7sc00284j

Authors: Babu Sudhamalla, Debasis Dey, Megan Breski, Tiffany Nguyen, Kabirul Islam

Institution: University of Pittsburgh

Language: English

Topic: Protein Degradation and Inhibitors

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: diamond

Funders: University of Pittsburgh, Cancer Institute, University of Pittsburgh, National Cancer Institute, National Institute of General Medical Sciences

Awards: G6966134840, Site-Specific Photochemistry on Epigenetic Readers for Interactome Profiling, Cancer Center Support Grant, G948547148