<br>植原体 SAP05 在不依赖于泛素的蛋白质降解中识别植物 Rpn10 的结构基础,iScience

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植原体 SAP05 在不依赖于泛素的蛋白质降解中识别植物 Rpn10 的结构基础
iScience ( IF 4.6 ) Pub Date : 2024-01-12 , DOI: 10.1016/j.isci.2024.108892
Liying Zhang _{1,

2} , Yunxiang Du _{1,

2} , Qian Qu ₁ , Qingyun Zheng _{1,

2}

Affiliation

除了传统的泛素依赖性蛋白酶体降解之外，数以千计的真核蛋白质可能会发生不依赖于泛素的蛋白酶体降解（UbInPD）。由植原体分泌的病原体编码效应蛋白 SAP05，可以劫持蛋白酶体的 Rpn10 亚基，并靶向降解 GATA 结合因子 (GATA) 或鳞状启动子结合蛋白样 (SPL) 转录因子 (TF)，而无需泛素或额外的蛋白酶体穿梭因子。为了解释 SAP05 如何绕过泛素依赖性途径靶向降解，我们确定了 Rpn10 和 SAP05 或 SAP05 之间复合物的晶体结构，该结构显示了以前未知的识别界面。序列比对和结构生物学证据表明，这种相互作用在各种 SAP05 同源物中高度保守，表明植物感染的一般模式。将复杂结构与植物蛋白酶体对接后，SAP05 靠近三磷酸腺苷酶 (ATPase) 中心孔，足以使底物进行降解过程，这表明具有分子胶样作用，可以桥接靠近蛋白酶体 ATPase 中心孔的 TF用于直接降解。

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Structure basis for recognition of plant Rpn10 by phytoplasma SAP05 in ubiquitin-independent protein degradation

Besides traditional ubiquitin-dependent proteasome degradation, thousands of eukaryotic proteins more than previously appreciated could undergo ubiquitin-independent proteasomal degradation (UbInPD). A pathogen-encoded effector protein SAP05 secreted by phytoplasma, could hijack hostage Rpn10 subunit of proteasome derived from and target the degradation of GATA BINDING FACTOR (GATA) or SQUAMOSA-PROMOTER BINDING PROTEIN-LIKE (SPL) transcription factors (TFs) without ubiquitin or additional proteasome shuttle factors. To explain how could SAP05 target the degradation bypassing the ubiquitin-dependent pathway, we have determined the crystal structure of the complex between Rpn10 and SAP05 or SAP05, which showed a previously unknown recognition interface. Sequence alignment and structural biological evidence showed that this interaction is highly conserved in various SAP05 homologs, suggesting a general mode in plant infection. After docking the complex structure to the plant proteasome, SAP05 was near to the adenosine triphosphatase (ATPase) central pore and enough to submit substrate to degradation process, which suggested a molecular glue-like role to bridge TFs close to the ATPase central pore of proteasomes for the direct degradation.

更新日期：2024-01-12

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