期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 18, 期 6, 页码 643-U34出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2056
关键词
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资金
- Howard Hughes Medical Institute
- Rockefeller University
- US National Science Foundation [BES-0620813]
- National Institutes of Health [R01 GM087977]
The nuclear pore complex (NPC) perforates the nuclear envelope to facilitate selective transport between nucleus and cytoplasm. The NPC is composed of multiple copies of similar to 30 different proteins, termed nucleoporins, whose arrangement within the NPC is an important unsolved puzzle in structural biology. Various alternative models for NPC architecture have been proposed but not tested experimentally in intact NPCs. We present a method using polarized fluorescence microscopy to investigate nucleoporin orientation in live yeast and mammalian cells. Our results support an arrangement of both yeast Nic96 and human Nup133-Nup107 in which their long axes are approximately parallel to the nuclear envelope plane. The method we developed can complement X-ray crystallography and electron microscopy to generate a high-resolution map of the entire NPC, and may be able to monitor nucleoporin rearrangements during nucleocytoplasmic transport and NPC assembly. This strategy can also be adapted for other macromolecular machines.
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