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

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 () and Cheng Dong ()
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Xiaojie Yan: Tianjin Medical University
Xinxin Yuan: Tianjin Medical University
Jianke Lv: Tianjin Medical University
Bing Zhang: Tianjin Medical University
Yongle Huang: Tianjin Medical University
Qianqian Li: 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
Cheng Dong: Tianjin Medical University

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-45521-7

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