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Nuclear condensates of p300 formed though the structured catalytic core can act as a storage pool of p300 with reduced HAT activity

Author

Listed:
  • Yi Zhang

    (University of Colorado School of Medicine)

  • Kyle Brown

    (University of Colorado)

  • Yucong Yu

    (Van Andel Research Institute)

  • Ziad Ibrahim

    (University of Leicester)

  • Mohamad Zandian

    (University of Colorado School of Medicine)

  • Hongwen Xuan

    (Van Andel Research Institute)

  • Steven Ingersoll

    (University of Colorado)

  • Thomas Lee

    (University of Colorado)

  • Christopher C. Ebmeier

    (University of Colorado)

  • Jiuyang Liu

    (University of Colorado School of Medicine)

  • Daniel Panne

    (University of Leicester)

  • Xiaobing Shi

    (Van Andel Research Institute)

  • Xiaojun Ren

    (University of Colorado)

  • Tatiana G. Kutateladze

    (University of Colorado School of Medicine)

Abstract

The transcriptional co-activator and acetyltransferase p300 is required for fundamental cellular processes, including differentiation and growth. Here, we report that p300 forms phase separated condensates in the cell nucleus. The phase separation ability of p300 is regulated by autoacetylation and relies on its catalytic core components, including the histone acetyltransferase (HAT) domain, the autoinhibition loop, and bromodomain. p300 condensates sequester chromatin components, such as histone H3 tail and DNA, and are amplified through binding of p300 to the nucleosome. The catalytic HAT activity of p300 is decreased due to occlusion of the active site in the phase separated droplets, a large portion of which co-localizes with chromatin regions enriched in H3K27me3. Our findings suggest a model in which p300 condensates can act as a storage pool of the protein with reduced HAT activity, allowing p300 to be compartmentalized and concentrated at poised or repressed chromatin regions.

Suggested Citation

  • Yi Zhang & Kyle Brown & Yucong Yu & Ziad Ibrahim & Mohamad Zandian & Hongwen Xuan & Steven Ingersoll & Thomas Lee & Christopher C. Ebmeier & Jiuyang Liu & Daniel Panne & Xiaobing Shi & Xiaojun Ren & T, 2021. "Nuclear condensates of p300 formed though the structured catalytic core can act as a storage pool of p300 with reduced HAT activity," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24950-8
    DOI: 10.1038/s41467-021-24950-8
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    Cited by:

    1. Ziad Ibrahim & Tao Wang & Olivier Destaing & Nicola Salvi & Naghmeh Hoghoughi & Clovis Chabert & Alexandra Rusu & Jinjun Gao & Leonardo Feletto & Nicolas Reynoird & Thomas Schalch & Yingming Zhao & Ma, 2022. "Structural insights into p300 regulation and acetylation-dependent genome organisation," Nature Communications, Nature, vol. 13(1), pages 1-23, December.
    2. Dustin C. Becht & Brianna J. Klein & Akinori Kanai & Suk Min Jang & Khan L. Cox & Bing-Rui Zhou & Sabrina K. Phanor & Yi Zhang & Ruo-Wen Chen & Christopher C. Ebmeier & Catherine Lachance & Maxime Gal, 2023. "MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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