Chemical biology approaches to study histone interactors. Author Antony Burton, Ghaith Hamza, Andrew Zhang, Tom Muir Publication Year 2021 Type Journal Article Abstract Protein-protein interactions (PPIs) in the nucleus play key roles in transcriptional regulation and ensure genomic stability. Critical to this are histone-mediated PPI networks, which are further fine-tuned through dynamic post-translational modification. Perturbation to these networks leads to genomic instability and disease, presenting epigenetic proteins as key therapeutic targets. This mini-review will describe progress in mapping the combinatorial histone PTM landscape, and recent chemical biology approaches to map histone interactors. Recent advances in mapping direct interactors of histone PTMs as well as local chromatin interactomes will be highlighted, with a focus on mass-spectrometry based workflows that continue to illuminate histone-mediated PPIs in unprecedented detail. Keywords Protein Binding, Crystallography, X-Ray, Mass Spectrometry, Protein Processing, Post-Translational, Histones Journal Biochem Soc Trans Volume 49 Issue 5 Pages 2431-2441 Date Published 2021 Nov 01 ISSN Number 1470-8752 DOI 10.1042/BST20210772 Alternate Journal Biochem Soc Trans PMCID PMC9785950 PMID 34709376 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML