一个球状折叠蛋白质的相分离和聚合 小型乌比奎丁类修饰剂1 (SUMO1)
Simran Arora1, Debsankar Saha Roy1, Sudipta Maiti1
1Department of Chemical Sciences, Tata Institute of Fundamental Research, Dr. Homi Bhabha Road, Colaba, Mumbai 400005, India.
The journal of physical chemistry letters
|October 2, 2023
概括
折叠的蛋白质,如SUMO1,可以通过液-液相分离 (LLPS) 快速形成类似液体的冷凝物. 这挑战了只有无序的蛋白质才能驱动细胞中的凝结物形成的观点.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 生物物理学的生物物理.
背景情况:
- 液体-液体相分离 (LLPS) 通过生物分子凝聚物驱动细胞组织.
- 内在无序的蛋白质 (IDP) 是LLPS的主要驱动因素.
- 折叠蛋白质,如SUMO在LLPS中的作用正在调查中.
研究的目的:
- 为了研究折叠蛋白质SUMO1接受LLPS的能力.
- 阐明SUMO1在凝结物形成中的机制和结构贡献.
- 探索折叠蛋白质在没有细胞膜的组件中的含义.
主要方法:
- 在生理条件下使用惰性 crowders 诱导 SUMO1 阶段分离.
- 无标签的生物物理技术,包括托芬光和拉曼光谱.
- 对SUMO1变体缺乏其N终端无序区域的分析.
主要成果:
- SUMO1 经历了快速相位分离到类似液体的冷凝物.
- 观察到SUMO1凝聚物的依赖时间的形状变化和聚合.
- SUMO1 的结构域对于其相位过渡特性至关重要.
结论:
- 折叠蛋白质,以SUMO1为例,具有参与LLPS的能力.
- SUMO1的结构区域对其相位分离行为做出了重大贡献.
- 研究结果表明,折叠蛋白在调节细胞凝聚物和IDP行为方面起着更广泛的作用.
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