IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-45521-7.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-45521-7
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-45521-7?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    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.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Indrajit Sahu & Sachitanand M. Mali & Prasad Sulkshane & Cong Xu & Andrey Rozenberg & Roni Morag & Manisha Priyadarsini Sahoo & Sumeet K. Singh & Zhanyu Ding & Yifan Wang & Sharleen Day & Yao Cong & O, 2021. "The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag," Nature Communications, Nature, vol. 12(1), pages 1-21, December.
    2. Nathan Jespersen & Kai Ehrenbolger & Rahel R. Winiger & Dennis Svedberg & Charles R. Vossbrinck & Jonas Barandun, 2022. "Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Ian Cooney & Heidi L. Schubert & Karina Cedeno & Olivia N. Fisher & Richard Carson & John C. Price & Christopher P. Hill & Peter S. Shen, 2024. "Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    4. Ka Ying Sharon Hung & Sven Klumpe & Markus R. Eisele & Suzanne Elsasser & Geng Tian & Shuangwu Sun & Jamie A. Moroco & Tat Cheung Cheng & Tapan Joshi & Timo Seibel & Duco Dalen & Xin-Hua Feng & Ying L, 2022. "Allosteric control of Ubp6 and the proteasome via a bidirectional switch," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    5. Yang Xu & Han Han & Ian Cooney & Yuxuan Guo & Noah G. Moran & Nathan R. Zuniga & John C. Price & Christopher P. Hill & Peter S. Shen, 2022. "Active conformation of the p97-p47 unfoldase complex," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    6. Maximilian Fottner & Maria Weyh & Stefan Gaussmann & Dominic Schwarz & Michael Sattler & Kathrin Lang, 2021. "A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45521-7. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.