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Home > Publications

Interplay of condensation and chromatin binding underlies BRD4 targeting

Authors Amy R Strom , Jorine M Eeftens  , Yury Polyachenko , Claire J Weaver  , Hans-Frederick Watanabe , Dan Bracha  , Natalia D Orlovsky  , Chanelle C Jumper  , William M Jacobs , Clifford P Brangwynne   
Details Amy R Strom et al; Mol Biol Cell; 2024;
DOI 10.1091/mbc.E24-01-0046
Topics
  • Biology and Physics of Condensates
  • Biotechnology and engineering
Tags
  • Biomolecular condensates
  • Intrinsically disordered proteins
  • Low complexity sequence domains
  • Phase separation
  • Transcriptional condensates
Source View on PubMed
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“The role of substrate-binding interactions in regulating the formation and function of biomolecular condensates is under-explored.

Studying BET family transcription factor BRD4, the authors performed coarse-grained simulations and live cell experiments to elucidate the kinetic and thermodynamic properties of condensation that are affected by acetylated chromatin binding. They found that acetylated chromatin binding targets and enhances BRD4 condensation.

This provides a molecular and physical explanation of the relationship between nuclear condensates and epigenetically modified chromatin that results in their mutual spatiotemporal regulation, suggesting that epigenetic modulation is an important mechanism by which transcriptional condensates target specific chromatin loci.”

Contributed by Yurong Fei-Bloom

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