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Molecular basis of SAP05-mediated ubiquitin-independent proteasomal degradation of transcription factors

Author

Listed:
  • Xiaojie Yan

    (Tianjin Medical University
    Tianjin Medical University)

  • Xinxin Yuan

    (Tianjin Medical University
    Tianjin Medical University
    Tianjin Medical University General Hospital)

  • Jianke Lv

    (Tianjin Medical University
    Tianjin Medical University)

  • Bing Zhang

    (Tianjin Medical University
    Tianjin Medical University)

  • Yongle Huang

    (Tianjin Medical University)

  • Qianqian Li

    (Tianjin Medical University
    Tianjin Medical University)

  • Jinfeng Ma

    (Tianjin Medical University General Hospital)

  • Yanran Li

    (Tianjin Medical University)

  • Xiaolu Wang

    (Tianjin Medical University)

  • Yao Li

    (Tianjin Medical University)

  • Ying Yu

    (Tianjin Medical University)

  • Quanyan Liu

    (Tianjin Medical University General Hospital)

  • Tong Liu

    (Second Hospital of Tianjin Medical University)

  • Wenyi Mi

    (Tianjin Medical University
    Tianjin Medical University)

  • Cheng Dong

    (Tianjin Medical University
    Tianjin Medical University
    Tianjin Medical University General Hospital
    Second Hospital of Tianjin Medical University)

Abstract

SAP05, a secreted effector by the obligate parasitic bacteria phytoplasma, bridges host SPL and GATA transcription factors (TFs) to the 26 S proteasome subunit RPN10 for ubiquitination-independent degradation. Here, we report the crystal structures of SAP05 in complex with SPL5, GATA18 and RPN10, which provide detailed insights into the protein-protein interactions involving SAP05. SAP05 employs two opposing lobes with an acidic path and a hydrophobic path to contact TFs and RPN10, respectively. Our crystal structures, in conjunction with mutagenesis and degradation assays, reveal that SAP05 targets plant GATAs but not animal GATAs dependent on their direct salt-bridged electrostatic interactions. Additionally, SAP05 hijacks plant RPN10 but not animal RPN10 due to structural steric hindrance and the key hydrophobic interactions. This study provides valuable molecular-level information into the modulation of host proteins to prevent insect-borne diseases.

Suggested Citation

  • Xiaojie Yan & Xinxin Yuan & Jianke Lv & Bing Zhang & Yongle Huang & Qianqian Li & Jinfeng Ma & Yanran Li & Xiaolu Wang & Yao Li & Ying Yu & Quanyan Liu & Tong Liu & Wenyi Mi & Cheng Dong, 2024. "Molecular basis of SAP05-mediated ubiquitin-independent proteasomal degradation of transcription factors," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45521-7
    DOI: 10.1038/s41467-024-45521-7
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    References listed on IDEAS

    as
    1. Neha Rani & Annette Aichem & Gunter Schmidtke & Stefan G. Kreft & Marcus Groettrup, 2012. "FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis," Nature Communications, Nature, vol. 3(1), pages 1-11, January.
    2. Yuanchen Dong & Shuwen Zhang & Zhaolong Wu & Xuemei Li & Wei Li Wang & Yanan Zhu & Svetla Stoilova-McPhie & Ying Lu & Daniel Finley & Youdong Mao, 2019. "Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome," Nature, Nature, vol. 565(7737), pages 49-55, January.
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