Chemical biology approaches to study histone interactors. (1st November 2021)

• Record Type: Journal Article
• Authors: Burton, Antony J.; Hamza, Ghaith M.; Zhang, Andrew X.; Muir, Tom W.
• Is Part Of: Biochemical Society transactions. Volume 49:Number 5(2021)
• Page Start: 2431
• Page End: 2441
• Publication Date: 2021-11-01
• Subjects: chemical biology -- chromatin -- epigenetics -- mass spectrometry -- post translational modification -- protein–protein interactions; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20210772
• Languages: English
• ISSNs: 0300-5127

Abstract

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.