期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 58, 期 37, 页码 13004-13008出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201905685
关键词
DNA-PAINT; genetically encoded tags; nuclear pore complex; single-molecule imaging; super-resolution microscopy
资金
- German Research Foundation through the Emmy Noether Program (DFG) [JU 2957/1-1, SFB1032]
- European Research Council through an ERC [680241]
- ERC Consolidator Grant (ERC) [CoG-724489]
- National Institutes of Health Common Fund 4D Nucleome Program [U01 EB021223/U01 DA047728]
- European Molecular Biology Laboratory (EMBL)
- Max Planck Foundation
- Max Planck Society
- QBM graduate school
- International Max Planck Research School for Molecular and Cellular Life Sciences (IMPRS-LS)
- Boehringer Ingelheim Fonds
- Allen Distinguished Investigator Program through The Paul G. Allen Frontiers Group
The nuclear pore complex (NPC) is one of the largest and most complex protein assemblies in the cell and, among other functions, serves as the gatekeeper of nucleocytoplasmic transport. Unraveling its molecular architecture and functioning has been an active research topic for decades with recent cryogenic electron microscopy and super-resolution studies advancing our understanding of the architecture of the NPC complex. However, the specific and direct visualization of single copies of NPC proteins is thus far elusive. Herein, we combine genetically-encoded self-labeling enzymes such as SNAP-tag and HaloTag with DNA-PAINT microscopy. We resolve single copies of nucleoporins in the human Y-complex in three dimensions with a precision of circa 3 nm, enabling studies of multicomponent complexes on the level of single proteins in cells using optical fluorescence microscopy.
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