Chemical biology approaches to study histone interactors

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 geno...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 49; no. 5; p. 2431
Main Authors Burton, Antony J, Hamza, Ghaith M, Zhang, Andrew X, Muir, Tom W
Format Journal Article
LanguageEnglish
Published England 01.11.2021
Subjects
Crystallography, X-Ray - methods
Histones - metabolism
Mass Spectrometry - methods
Protein Binding
Protein Processing, Post-Translational
protein–protein interactions
post translational modification
mass spectrometry
chemical biology
chromatin
epigenetics
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Summary: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.
ISSN:1470-8752
DOI:10.1042/BST20210772