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度依赖突变扫描探测酵母中α-核素的细胞折叠景观

Daeun Noh, Robert W Newberry

bioRxiv : the preprint server for biology

|September 5, 2025

概括

帕金森病蛋白α-同核素的错误折叠取决于度. 在酵母中深度突变扫描显示有毒,膜结合状态是受欢迎的, 但突变可以破坏这种有毒聚合.

科学领域:

神经退行性疾病研究
蛋白质错误折叠和聚合
细胞生物学和生物物理学

背景情况:

阿尔法同核素 (α-synuclein) 的错误折叠和聚合是帕金森病的关键病因.
蛋白质度显著影响错折和病理,但细胞机制尚不清楚.
传统的结构生物学方法在生物系统中缺乏解决方案.

研究的目的:

研究细胞度如何影响α-synuclein的折叠形态.
应用深度突变扫描来探测活体酵母模型中的α-synuclein折叠.
了解毒性α-synuclein构造中的度依赖性变化.

主要方法:

在酵母模型中对α-synuclein进行深度突变扫描.
对不同细胞度的折叠状态和膜结合倾向的分析.
影响膜亲和力的突变及其对毒性的特征.

主要成果:

在不同度下,α-synuclein强烈支持有毒的,与膜结合的两螺旋.
减少膜亲和力的突变破坏了有毒折叠平衡.
与野生类型相比,减少亲和度变体表现出明显的度依赖行为.

结论:

深度突变扫描为活细胞中的蛋白质折叠提供了高分辨率的洞察力.
细胞度极大地影响了有毒α-同核素构成的群体.
了解这些折叠动态对于研究像帕金森病这样的蛋白质错折疾病至关重要.

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