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H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation

Author

Listed:
  • Anfeng Luo

    (Capital Medical University)

  • Jingwei Kong

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Jun Chen

    (Capital Medical University)

  • Xue Xiao

    (Chinese Academy of Sciences)

  • Jie Lan

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Xiaorong Li

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Cuifang Liu

    (Institute of Biophysics, Chinese Academy of Sciences)

  • Peng-Ye Wang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences
    Songshan Lake Materials Laboratory)

  • Guohong Li

    (University of Chinese Academy of Sciences
    Institute of Biophysics, Chinese Academy of Sciences)

  • Wei Li

    (Chinese Academy of Sciences
    Institute of Biophysics, Chinese Academy of Sciences
    Songshan Lake Materials Laboratory)

  • Ping Chen

    (Capital Medical University
    Institute of Biophysics, Chinese Academy of Sciences)

Abstract

Histone H2B mono-ubiquitination at lysine 120 (ubH2B) has been found to regulate transcriptional elongation by collaborating with the histone chaperone FACT (Facilitates Chromatin Transcription) and plays essential roles in chromatin-based transcriptional processes. However, the mechanism of how ubH2B directly collaborates with FACT at the nucleosome level still remains elusive. In this study, we demonstrate that ubH2B impairs the mechanical stability of the nucleosome and helps to recruit FACT by enhancing the binding of FACT on the nucleosome. FACT prefers to bind and deposit H2A-ubH2B dimers to form an intact nucleosome. Strikingly, the preferable binding of FACT on ubH2B-nucleosome greatly enhances nucleosome stability and maintains its integrity. The stable altered nucleosome state obtained by ubH2B and FACT provides a key platform for gene transcription, as revealed by genome-wide and time-course ChIP-qPCR analyses. Our findings provide mechanistic insights of how ubH2B directly collaborates with FACT to regulate nucleosome dynamics for gene transcription.

Suggested Citation

  • Anfeng Luo & Jingwei Kong & Jun Chen & Xue Xiao & Jie Lan & Xiaorong Li & Cuifang Liu & Peng-Ye Wang & Guohong Li & Wei Li & Ping Chen, 2023. "H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36467-3
    DOI: 10.1038/s41467-023-36467-3
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    References listed on IDEAS

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    3. Robert K. McGinty & Jaehoon Kim & Champak Chatterjee & Robert G. Roeder & Tom W. Muir, 2008. "Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation," Nature, Nature, vol. 453(7196), pages 812-816, June.
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