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在液-液相分离之前的CPEB4异型集群的核心外模型

Maria Oranges¹, Chandrima Jash¹, Gonen Golani²

¹Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.

Biophysical journal

|June 29, 2024

概括

细胞质多基化元素结合-4蛋白 (CPEB4) N-终端域形成可溶性蛋白质集群,先于液-液相分离 (LLPS). 这些群体表现出核心外结构,这表明. 内部有不同的蛋白质构造.

科学领域:

生物物理学的生物物理.
分子生物学分子生物学
蛋白质动力学蛋白质动力学

背景情况:

液-液相分离 (LLPS) 对于细胞组织至关重要.
细胞质多基化元素结合-4蛋白 (CPEB4) N-终端域 (CPEB4_NTD) 和其Exon4缺少异型 (CPEB4Δ4_NTD) 经历LLPS.
与典型系统不同,它们的LLPS前状态涉及可溶性蛋白质集群.

研究的目的:

阐明CPEB4_NTD和CPEB4Δ4_NTD蛋白质集群的内部结构和形成机制.
为了研究这些蛋白质在集群和同动物中的独特动态性质.
了解离子强度和添加剂在集群形成中的作用.

主要方法:

动态光散射 (DLS) 和原子力显微镜 (AFM) 用于集群大小分析.
电子偏磁共振 (EPR) 光谱对自旋标记蛋白质进行探测动力学.
统计建模来描述集群结构.集群结构.
研究离子强度和1,6-二醇的影响.

主要成果:

在LLPS之前,CPEB4_NTD和CPEB4Δ4_NTD都形成了集群 (35-80 nm).
EPR揭示了两个不同的蛋白质动态群体在集群和协同生.
DLS数据支持核心集群结构,与统计模型一致.
在异构体之间观察到集群和同体属性的差异.
协同生可能是这些集群的聚合物.

结论:

CPEB4_NTD和CPEB4Δ4_NTD集群具有具有不同的蛋白质构造的核心外结构.
蛋白质动力学在群体和同体内有所不同,表明了复杂的内部组织.
这些系统中的LLPS涉及中间集群状态,挑战传统模型.
凝聚生物可以通过这些预先形成的集群的聚合而形成.

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