Most RNA-binding modules are small and bind few nucleotides. RNA-binding proteins typically attain the physiological specificity and affinity for their RNA targets by combining several RNA-binding modules. Here, we review how disordered linkers connecting RNA-binding modules govern the specificity and affinity of RNA–protein interactions by regulating the effective concentration of these modules and their relative orientation. RNA-binding proteins also often contain extended intrinsically disordered regions that mediate protein–protein and RNA–protein interactions with multiple partners. We discuss how these regions can connect proteins and RNA resulting in heterogeneous higher-order assemblies such as membrane-less compartments and amyloid-like structures that have the characteristics of multi-modular entities. The assembled state generates additional RNA-binding specificity and affinity properties that contribute to further the function of RNA-binding proteins within the cellular environment.

大多数 RNA 结合模块都很小，只结合很少的核苷酸。RNA 结合蛋白通常通过组合几个 RNA 结合模块来获得对其 RNA 靶标的生理特异性和亲和力。在这里，我们回顾了连接 RNA 结合模块的无序接头如何通过调节这些模块的有效浓度及其相对方向来控制 RNA-蛋白质相互作用的特异性和亲和力。RNA 结合蛋白通常还包含扩展的内在无序区域，这些区域介导蛋白质-蛋白质和 RNA-蛋白质与多个伙伴的相互作用。我们讨论这些区域如何连接蛋白质和 RNA，从而产生异质的高阶组件，例如具有多模块实体特征的无膜隔室和类淀粉样结构。