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Molecular basis for cysteine oxidation by Plant Cysteine Oxidases from Arabidopsis thaliana
Journal of Structural Biology ( IF 3 ) Pub Date : 2020-11-15 , DOI: 10.1016/j.jsb.2020.107663
Zhenzhen Chen 1 , Qiong Guo 2 , Gao Wu 3 , Jie Wen 3 , Shanhui Liao 2 , Chao Xu 2
Affiliation  

Plant Cysteine Oxidases (PCOs) play important roles in controlling the stability of Group VII ethylene response factors (ERF-VIIs) via N-Arg/degron pathway through catalyzing the oxidation of their N-Cys for subsequent Arginyl-tRNA--protein transferase 1 (ATE1) mediated arginine installation. Here we presented structures of PCO2, PCO4, and PCO5 from Arabidopsis thaliana (AtPCOs) and examined their in vitro activity by MS. On the basis of Tris-bound AtPCO2, we modelled the Cys-bound AtPCO2 structure and identified key residues involved in N-Cys oxidation. Alanine substitution of potential N-Cys interaction residues impaired the activity of AtPCO5 remarkably. The structural research, complemented by mutagenesis and mass spectrometry experiments, not only uncovers the substrate recognition and catalytic mode by AtPCOs, but also sheds light on the future design of potent inhibitors for plant cysteine oxidases.



中文翻译:

拟南芥植物半胱氨酸氧化酶氧化半胱氨酸的分子基础

植物半胱氨酸氧化酶 (PCO) 在通过 N-Arg/degron 途径通过催化其 N-Cys 氧化用于随后的精氨酰-tRNA-蛋白转移酶 1 来控制第 VII 组乙烯反应因子 (ERF-VIIs) 的稳定性方面发挥重要作用(ATE1) 介导的精氨酸安装。在这里,我们展示了来自拟南芥( At PCOs)的 PCO2、PCO4 和 PCO5 的结构,并通过 MS检测了它们的体外活性。在 Tris-bound At PCO2的基础上,我们模拟了 Cys-bound At PCO2 结构并确定了参与 N-Cys 氧化的关键残基。潜在的 N-Cys 相互作用残基的丙氨酸取代损害了At的活性PCO5 显着。结构研究,辅以诱变和质谱实验,不仅揭示了At PCOs的底物识别和催化模式,而且为植物半胱氨酸氧化酶的有效抑制剂的未来设计提供了启示。

更新日期:2020-11-15
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