The role of disorder in RNA binding affinity and specificity.

The role of disorder in RNA binding affinity and specificity.
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DOI:
10.1098/rsob.200328
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发表时间:
2020-12
期刊:
影响因子:
5.8
通讯作者:
Berchowitz LE
Berchowitz LE
中科院分区:
生物学2区
文献类型:
--
作者:
Ottoz DSM;Berchowitz LE

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大多数RNA结合模块都很小,结合的核苷酸很少。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,我们回顾如何无序连接连接RNA结合模块管理的特异性和亲和力的RNA-蛋白质相互作用,通过调节这些模块的有效浓度和它们的相对方向。RNA结合蛋白通常还含有延伸的内在无序区域,其介导蛋白质-蛋白质和RNA-蛋白质与多个伴侣的相互作用。我们讨论了这些区域如何连接蛋白质和RNA,从而产生具有多模块实体特征的非均质高阶组装体,如无膜隔室和淀粉样结构。组装状态产生额外的RNA结合特异性和亲和力特性,有助于RNA结合蛋白在细胞环境中的进一步功能。
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.
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