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Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation

Author

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  • Yongming Du

    (The University of Hong Kong)

  • Yinxia Yan

    (The University of Hong Kong)

  • Si Xie

    (The University of Hong Kong)

  • Hao Huang

    (The City University of Hong Kong)

  • Xin Wang

    (The City University of Hong Kong)

  • Ray Kit Ng

    (The University of Hong Kong)

  • Ming-Ming Zhou

    (Icahn School of Medicine at Mount Sinai)

  • Chengmin Qian

    (The University of Hong Kong)

Abstract

Spindlin1 is a unique multivalent epigenetic reader that facilitates ribosomal RNA transcription. In this study, we provide molecular and structural basis by which Spindlin1 acts in complex with C11orf84 to preferentially recognize non-canonical bivalent mark of trimethylated lysine 4 and lysine 9 present on the same histone H3 tail (H3K4me3K9me3). We demonstrate that C11orf84 binding stabilizes Spindlin1 and enhances its association with bivalent H3K4me3K9me3 mark. The functional analysis suggests that Spindlin1/C11orf84 complex can displace HP1 proteins from H3K4me3K9me3-enriched rDNA loci, thereby facilitating the conversion of these poised rDNA repeats from the repressed state to the active conformation, and the consequent recruitment of RNA Polymerase I for rRNA transcription. Our study uncovers a previously unappreciated mechanism of bivalent H3K4me3K9me3 recognition by Spindlin1/C11orf84 complex required for activation of rRNA transcription.

Suggested Citation

  • Yongming Du & Yinxia Yan & Si Xie & Hao Huang & Xin Wang & Ray Kit Ng & Ming-Ming Zhou & Chengmin Qian, 2021. "Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21236-x
    DOI: 10.1038/s41467-021-21236-x
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    Cited by:

    1. Fen Yang & Jianji Chen & Bin Liu & Guozhen Gao & Manu Sebastian & Collene Jeter & Jianjun Shen & Maria D. Person & Mark T. Bedford, 2021. "SPINDOC binds PARP1 to facilitate PARylation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Wei Liu & Qiyan Yao & Xiaonan Su & Yafang Deng & Mo Yang & Bo Peng & Fan Zhao & Chao Du & Xiulan Zhang & Jinsong Zhu & Daliang Wang & Wenhui Li & Haitao Li, 2023. "Molecular insights into Spindlin1-HBx interplay and its impact on HBV transcription from cccDNA minichromosome," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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