在体上菌体L装饰蛋白的模板三元化
Brianna M Woodbury1, Rebecca L Newcomer1, Andrei T Alexandrescu1
1Department of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Rd, Storrs, CT, 06269-3125, USA.
bioRxiv : the preprint server for biology
|September 16, 2024
概括
菌体L装饰蛋白 (Dec) 形成了一个稳定的同位素,对囊稳定至关重要. 体模板化在体内动态加快了Decrimer组件的组装,展示了一个独特的寡合体折叠机制.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 生物化学 生物化学
背景情况:
- 体L装饰蛋白 (Dec) 形成一个同位素,对稳定体体具有至关重要的作用.
- Dec 具有N端OB折叠域用于维相互作用和C端尖峰用于三元体稳定.
研究的目的:
- 为了研究Dec的C端尖端在囊结合中的作用.
- 在生物体中阐明 Dec Trimer 的组装机制.
主要方法:
- 局部定向的突变发生,以产生缺乏C端尖端 (Dec Δ99-134) 的Dec突变.
- 脱剂的pH诱导解离和体外重组实验.
- 在不同pH条件下对Dec单体和三元体结构的分析.
主要成果:
- Dec的OB折叠域独立折叠,但C终端尖端对于结合菌体P22病毒来说至关重要.
- 在低pH (<2) 时,dec trimers 分解成单体,具有未折叠的尖峰.
- 缓慢的体外三元体形成发生在中性pH (6) 时,这表明体内模板组装.
结论:
- Dec的C端尖峰对于稳定的囊相互作用至关重要.
- 体囊体模板化在体内动力学上加速了Dectrimer组装,支持了热力学假设.
- 体模板为Dec提供了灵活性,可以在体L体上结合准对称的位点.
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