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

Publication Type:

Journal Article


Nat Commun, Volume 11, Issue 1, p.6179 (2020)


<p>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.</p>

6X06 (Nup1201–757-VHH-SAN10/11), 6X07 (Nic96186–839-VHH-SAN12), 6X08 (Nup851–564-Seh1-VHH-SAN2)