Journal
BIOPHYSICAL JOURNAL
Volume 99, Issue 6, Pages 1706-1717Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2010.06.075
Keywords
-
Categories
Funding
- National Institutes of Health [R01 GM087977]
- Rockefeller University
- Howard Hughes Medical Institute
Ask authors/readers for more resources
We present a new approach for studying individual protein domains within the nuclear pore complex (NPC) using fluorescence polarization microscopy. The NPC is a large macromolecular complex, the size and complexity of which presents experimental challenges. Using fluorescence anisotropy and exploiting the symmetry of the NPC and its organization in the nuclear envelope, we have resolved order and disorder of individual protein domains. Fluorescently tagging specific domains of individual nucleoporins revealed both rigid and flexible domains: the tips of the FG domains are disordered, whereas the NPC-anchored domains are ordered. Our technique allows the collection of structural information in vivo, providing the ability to probe the organization of protein domains within the NPC. This has particular relevance for the FG domain nucleoporins, which are crucial for nucleocytoplasmic transport.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available