Nature Communications (Dec 2022)
Structural insights into p300 regulation and acetylation-dependent genome organisation
- Ziad Ibrahim,
- Tao Wang,
- Olivier Destaing,
- Nicola Salvi,
- Naghmeh Hoghoughi,
- Clovis Chabert,
- Alexandra Rusu,
- Jinjun Gao,
- Leonardo Feletto,
- Nicolas Reynoird,
- Thomas Schalch,
- Yingming Zhao,
- Martin Blackledge,
- Saadi Khochbin,
- Daniel Panne
Affiliations
- Ziad Ibrahim
- Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester
- Tao Wang
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Olivier Destaing
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Nicola Salvi
- Institut de Biologie Structurale, CNRS, CEA, UGA
- Naghmeh Hoghoughi
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Clovis Chabert
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Alexandra Rusu
- Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester
- Jinjun Gao
- Ben May Department of Cancer Research, The University of Chicago
- Leonardo Feletto
- Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester
- Nicolas Reynoird
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Thomas Schalch
- Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester
- Yingming Zhao
- Ben May Department of Cancer Research, The University of Chicago
- Martin Blackledge
- Institut de Biologie Structurale, CNRS, CEA, UGA
- Saadi Khochbin
- CNRS UMR 5309, INSERM U1209, Université Grenoble Alpes, Institute for Advanced Biosciences
- Daniel Panne
- Leicester Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester
- DOI
- https://doi.org/10.1038/s41467-022-35375-2
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 23
Abstract
Here the authors use structural analyses to show that an intrinsically disordered transcription activation domain in the oncogene BRD4-NUT binds to and activates p300. This in-turn drives formation of higher-order, acetylation-dependent chromatin condensates.
