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首页> 外文期刊>International Journal of Molecular Sciences >Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments
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Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments

机译：间隔和功能的核障碍：内核障碍和核内隔室中的蛋白质-蛋白质相互作用。

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The cell nucleus contains a number of membrane-less organelles or intra-nuclear compartments. These compartments are dynamic structures representing liquid-droplet phases which are only slightly denser than the bulk intra-nuclear fluid. They possess different functions, have diverse morphologies, and are typically composed of RNA (or, in some cases, DNA) and proteins. We analyzed 3005 mouse proteins localized in specific intra-nuclear organelles, such as nucleolus, chromatin, Cajal bodies, nuclear speckles, promyelocytic leukemia (PML) nuclear bodies, nuclear lamina, nuclear pores, and perinuclear compartment and compared them with ~29,863 non-nuclear proteins from mouse proteome. Our analysis revealed that intrinsic disorder is enriched in the majority of intra-nuclear compartments, except for the nuclear pore and lamina. These compartments are depleted in proteins that lack disordered domains and enriched in proteins that have multiple disordered domains. Moonlighting proteins found in multiple intra-nuclear compartments are more likely to have multiple disordered domains. Protein-protein interaction networks in the intra-nuclear compartments are denser and include more hubs compared to the non-nuclear proteins. Hubs in the intra-nuclear compartments (except for the nuclear pore) are enriched in disorder compared with non-nuclear hubs and non-nuclear proteins. Therefore, our work provides support to the idea of the functional importance of intrinsic disorder in the cell nucleus and shows that many proteins associated with sub-nuclear organelles in nuclei of mouse cells are enriched in disorder. This high level of disorder in the mouse nuclear proteins defines their ability to serve as very promiscuous binders, possessing both large quantities of potential disorder-based interaction sites and the ability of a single such site to be involved in a large number of interactions.
机译：细胞核包含许多无膜细胞器或核内区室。这些隔室是代表液滴相的动态结构，液滴相的密度仅比大块核内流体稍大。它们具有不同的功能，具有不同的形态，通常由RNA（或在某些情况下为DNA）和蛋白质组成。我们分析了位于特定核内细胞器中的3005种小鼠蛋白质，例如核仁，染色质，Cajal体，核斑，早幼粒细胞白血病（PML）核体，核层，核孔和核周区室，并将它们与〜29,863非小鼠蛋白质组中的核蛋白。我们的分析表明，除了核孔和薄层外，大多数内核隔室都富含内在疾病。这些区室缺少缺乏无序域的蛋白质，而富含具有多个无序域的蛋白质。在多个核内区室中发现的月光照蛋白更可能具有多个无序域。与非核蛋白相比，核内区室中的蛋白-蛋白相互作用网络更密集，并且包含更多的中枢。与非核集线器和非核蛋白相比，核内区室（除核孔外）的集线器富含无序。因此，我们的工作为内在疾病在细胞核中的功能重要性提供了支持，并且表明与小鼠细胞核中亚核细胞器相关的许多蛋白质都富含疾病。小鼠核蛋白中这种高水平的紊乱定义了它们充当非常混杂的结合物的能力，既具有大量潜在的基于疾病的相互作用位点，又具有单个此类位点参与大量相互作用的能力。

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