High mobility of proteins in the mammalian cell nucleus
High mobility of proteins in the mammalian cell nucleus
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DOI：
10.1038/35007077
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发表时间：
2000-04-06
期刊：
影响因子：
64.8
通讯作者：
Misteli, T
中科院分区：
文献类型：
--
作者：
Phair, RD;Misteli, T
哺乳动物细胞核包含许多亚区室，这些亚区室涉及转录和剪接等基本过程（1，2）。核隔室形成和维持的机制尚不清楚。更重要的是，我们不知道蛋白质如何在细胞核内移动。我们用光漂白技术测量了活细胞核中蛋白质的动力学性质。在这里，我们表明，蛋白质参与不同的核过程中迅速移动整个细胞核。蛋白质的运动不依赖于能量，这表明蛋白质可能使用被动的运动机制。蛋白质迅速与核区室结合和解离。使用动力学建模，我们确定了两个主要的核隔间的分子的停留时间和稳态通量。这些数据表明，许多核蛋白漫游细胞核在体内和核隔室是其“居民”与核质空间的稳态关联/解离的反映。我们的观察有概念上的影响，了解核结构和核过程是如何组织在体内。
The mammalian cell nucleus contains numerous sub-compartments, which have been implicated in essential processes such as transcription and splicing(1,2). The mechanisms by which nuclear compartments are formed and maintained are unclear. More fundamentally, it is not known how proteins move within the cell nucleus. We have measured the kinetic properties of proteins in the nucleus of living cells using photobleaching techniques. Here we show that proteins involved in diverse nuclear processes move rapidly throughout the entire nucleus. Protein movement is independent of energy, which indicates that proteins may use a passive mechanism of movement. Proteins rapidly associate and dissociate with nuclear compartments. Using kinetic modelling, we determined residence times and steady-state fluxes of molecules in two main nuclear compartments. These data show that many nuclear proteins roam the cell nucleus in vivo and that nuclear compartments are the reflection of the steady-state association/dissociation of its 'residents' with the nucleoplasmic space. Our observations have conceptual implications for understanding nuclear architecture and how nuclear processes are organized in vivo.