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A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure
Name
s41467-020-19884-6.pdf
Description
Published version
Size
7.92 MB
Format
Adobe PDF
Checksum (MD5)
42cc9b82110a84c6aa57ec13cefbcf26
Author(s)
Nordeen, Sarah A
Andersen, Kasper R
Knockenhauer, Kevin E
Ingram, Jessica R
Ploegh, Hidde L
Schwartz, Thomas U
Date Issued
2020
Journal
Nature Communications
Publisher
Springer Science and Business Media LLC
Version
Final published version
Abstract
© 2020, The Author(s). Nuclear pore complexes (NPCs) are the main conduits for molecular exchange across the nuclear envelope. The NPC is a modular assembly of ~500 individual proteins, called nucleoporins or nups. Most scaffolding nups are organized in two multimeric subcomplexes, the Nup84 or Y complex and the Nic96 or inner ring complex. Working in S. cerevisiae, and to study the assembly of these two essential subcomplexes, we here develop a set of twelve nanobodies that recognize seven constituent nucleoporins of the Y and Nic96 complexes. These nanobodies all bind specifically and with high affinity. We present structures of several nup-nanobody complexes, revealing their binding sites. Additionally, constitutive expression of the nanobody suite in S. cerevisiae detect accessible and obstructed surfaces of the Y complex and Nic96 within the NPC. Overall, this suite of nanobodies provides a unique and versatile toolkit for the study of the NPC.
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
10.1038/s41467-020-19884-6
