Rout M P, Aitchison J D, Suprapto A, Hjertaas K, Zhao Y, Chait B T
The Rockefeller University, New York, NY 10021, USA.
J Cell Biol. 2000 Feb 21;148(4):635-51. doi: 10.1083/jcb.148.4.635.
An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.
要理解核孔复合体(NPC)如何介导核质交换,需要全面了解NPC的分子组成,并知晓每个组分如何对这个大分子转运机器的整体结构发挥作用。因此,我们采用了一种全面的方法对酵母NPC的所有组分(核孔蛋白)进行分类。这包括鉴定高度富集的NPC组分中存在的所有蛋白质,确定其中哪些蛋白质是核孔蛋白,并将每个核孔蛋白定位在NPC内。利用这些数据,我们展示了酵母NPC的分子结构图谱,并为核质运输的布朗亲和门控机制提供了证据。