Structural insights into p300 regulation and acetylation-dependent genome organisation

Abstract excerpt

<h4>Summary</h4> Histone modifications are deposited by chromatin modifying enzymes and read out by proteins that recognize the modified state. BRD4-NUT is an oncogenic fusion protein of the acetyl lysine reader BRD4 that binds to the acetylase p300 and enables formation of long-range intra- and interchromosomal interactions. We here examine how acetylation reading and writing enable formation of such interaction...

Topics

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• Catalytic Domain
• Chromatin
• Crystallography, X-Ray
• Enzyme Stability
• p300-CBP Transcription Factors
• Protein Degradation and Inhibitors
• Protein Interaction Domains and Motifs
• Recombinant Fusion Proteins

Identifiers and source

Literature Corpus work

61ce4fe6-3f59-5705-97b4-c2e8c0e24073

DOI

10.1101/2022.03.14.484228