Amyloid-like protein assemblies have been associated with toxic phenotypes because of their repetitive and stable structure. However, evidence that cells exploit these structures to control function and activity of some proteins in response to stimuli has questioned this paradigm. How amyloid-like assembly can confer emergent functions and how cells couple assembly with environmental conditions remains unclear. Here, we study Rim4, an RNA-binding protein that forms translation-repressing assemblies during yeast meiosis. We demonstrate that in its assembled and repressive state, Rim4 binds RNA more efficiently than in its monomeric and idle state, revealing a causal connection between assembly and function. The Rim4-binding site location within the transcript dictates whether the assemblies can repress translation, underscoring the importance of the architecture of this RNA-protein structure for function. Rim4 assembly depends exclusively on its intrinsically disordered region and is prevented by the Ras/protein kinase A signaling pathway, which promotes growth and suppresses meiotic entry in yeast. Our results suggest a mechanism whereby cells couple a functional protein assembly with a stimulus to enforce a cell fate decision.

中文翻译：

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类淀粉样蛋白翻译抑制因子 Rim4 的组装和功能与营养条件相关

淀粉样蛋白组装体因其重复且稳定的结构而与毒性表型相关。然而，细胞利用这些结构来控制某些蛋白质响应刺激的功能和活性的证据对这种范式提出了质疑。淀粉样蛋白的组装如何赋予紧急功能以及细胞如何将组装与环境条件结合仍不清楚。在这里，我们研究了 Rim4，一种 RNA 结合蛋白，在酵母减数分裂过程中形成翻译抑制组件。我们证明，在组装和抑制状态下，Rim4 比在单体和闲置状态下更有效地结合 RNA，揭示了组装和功能之间的因果关系。转录本中 Rim4 结合位点的位置决定了组装体是否可以抑制翻译，强调了这种 RNA-蛋白质结构的结构对于功能的重要性。Rim4 的组装完全依赖于其本质上无序的区域，并受到 Ras/蛋白激酶 A 信号通路的阻止，该通路可促进酵母的生长并抑制减数分裂的进入。我们的结果提出了一种机制，细胞可以将功能性蛋白质组装体与刺激物结合起来，以强制执行细胞命运决定。