From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.
From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.
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DOI：
10.3390/ijms22031251
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发表时间：
2021-01-27
影响因子：
5.6
通讯作者：
Ross ED
中科院分区：
文献类型：
--
作者：
Fomicheva A;Ross ED
应激颗粒是响应细胞应激而形成的核糖核蛋白组装体。在应激颗粒蛋白质组中发现的许多RNA结合蛋白含有朊病毒样结构域（PrLD），其是组成上类似于酵母朊病毒结构域的低复杂性序列。这些PrLD中的一些突变与神经退行性疾病有关，包括肌萎缩侧索硬化症和额颞叶痴呆，并且与持续的应激颗粒积累有关。虽然压力颗粒和朊病毒都是大分子组装体，但它们的物理性质和复杂性都不同。朊病毒聚集体是高度稳定的均聚固体，而应力颗粒是由多价同型和异型相互作用驱动的复杂动态生物分子凝聚物。在这里，我们使用压力颗粒和酵母朊病毒作为一个范例，以研究不同的序列和组成特征的PrLD有助于不同类型的PrLD含组件。
Stress granules are ribonucleoprotein assemblies that form in response to cellular stress. Many of the RNA-binding proteins found in stress granule proteomes contain prion-like domains (PrLDs), which are low-complexity sequences that compositionally resemble yeast prion domains. Mutations in some of these PrLDs have been implicated in neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia, and are associated with persistent stress granule accumulation. While both stress granules and prions are macromolecular assemblies, they differ in both their physical properties and complexity. Prion aggregates are highly stable homopolymeric solids, while stress granules are complex dynamic biomolecular condensates driven by multivalent homotypic and heterotypic interactions. Here, we use stress granules and yeast prions as a paradigm to examine how distinct sequence and compositional features of PrLDs contribute to different types of PrLD-containing assemblies.
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