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Histone H2A monoubiquitination marks are targeted to specific sites by cohesin subunits in Arabidopsis

Author

Listed:
  • Yu Zhang

    (Shanghai Jiao Tong University)

  • Min Ma

    (Shanghai Jiao Tong University)

  • Meng Liu

    (Tongji University)

  • Aiqing Sun

    (Shanghai Jiao Tong University)

  • Xiaoyun Zheng

    (Shanghai Jiao Tong University)

  • Kunpeng Liu

    (Shanghai Jiao Tong University)

  • Chunmei Yin

    (Shanghai Jiao Tong University)

  • Chuanshun Li

    (Shanghai Jiao Tong University)

  • Cizhong Jiang

    (Tongji University)

  • Xiaoyu Tu

    (Shanghai Jiao Tong University)

  • Yuda Fang

    (Shanghai Jiao Tong University)

Abstract

Histone H2A monoubiquitination (H2Aub1) functions as a conserved posttranslational modification in eukaryotes to maintain gene expression and guarantee cellular identity. Arabidopsis H2Aub1 is catalyzed by the core components AtRING1s and AtBMI1s of polycomb repressive complex 1 (PRC1). Because PRC1 components lack known DNA binding domains, it is unclear how H2Aub1 is established at specific genomic locations. Here, we show that the Arabidopsis cohesin subunits AtSYN4 and AtSCC3 interact with each other, and AtSCC3 binds to AtBMI1s. H2Aub1 levels are reduced in atsyn4 mutant or AtSCC3 artificial microRNA knockdown plants. ChIP-seq assays indicate that most binding events of AtSYN4 and AtSCC3 are associated with H2Aub1 along the genome where transcription is activated independently of H3K27me3. Finally, we show that AtSYN4 binds directly to the G-box motif and directs H2Aub1 to these sites. Our study thus reveals a mechanism for cohesin-mediated recruitment of AtBMI1s to specific genomic loci to mediate H2Aub1.

Suggested Citation

  • Yu Zhang & Min Ma & Meng Liu & Aiqing Sun & Xiaoyun Zheng & Kunpeng Liu & Chunmei Yin & Chuanshun Li & Cizhong Jiang & Xiaoyu Tu & Yuda Fang, 2023. "Histone H2A monoubiquitination marks are targeted to specific sites by cohesin subunits in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36788-3
    DOI: 10.1038/s41467-023-36788-3
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