A Chemical Probe for Protein Crotonylation.

TitleA Chemical Probe for Protein Crotonylation.
Publication TypeJournal Article
Year of Publication2018
AuthorsBos, J, Muir, TW
JournalJ Am Chem Soc
Volume140
Issue14
Pagination4757-4760
Date Published2018 04 11
ISSN1520-5126
Abstract

Protein lysine crotonylation has emerged as an important post-translational modification (PTM) in the regulation of gene transcription through epigenetic mechanisms. Here we introduce a chemical probe, based on a water-soluble phosphine warhead, which reacts with the crotonyl modification. We show that this reagent is complementary to antibody-based tools allowing detection of endogenous cellular proteins such as histones carrying the crotonylation PTM. The tool is also used to show that the histone acylation activity of the transcriptional coactivator, p300, can be activated by pre-existing lysine crotonylation through a positive feedback mechanism. This reagent provides a versatile and sensitive probe for the analysis of this PTM.

DOI10.1021/jacs.7b13141
Alternate JournalJ. Am. Chem. Soc.
PubMed ID29584949