A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure.

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ID: 263797
2020
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Abstract
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.
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nordeen2020anature Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Nordeen, Sarah A;Andersen, Kasper R;Knockenhauer, Kevin E;Ingram, Jessica R;Ploegh, Hidde L;Schwartz, Thomas U;
Journal Nature communications
Year 2020
DOI
10.1038/s41467-020-19884-6
URL
Keywords
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