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© The Rockefeller University Press, 0021-9525/2000//41 $5.00
The Journal of Cell Biology, Volume 149, Number 1, , 2000 41-54

Original Article

Structure and Assembly of the Nup84p Complex



Symeon Siniossogloua, Malik Lutzmanna, Helena Santos-Rosaa, Kevin Leonardb, Shirley Muellerc, Ueli Aebic, and Ed Hurta

a Biochemie-Zentrum Heidelberg, D-69120 Heidelberg, Germany
b European Molecular Biology Laboratory, D-69117 Heidelberg, Germany
c Biozentrum, Maurice E. Müller Institute for Structural Biology, CH-4056 Basel, Switzerland
Biochemie-Zentrum Heidelberg, University of Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.49-6221-54-436949-6221-54-4173

cg5{at}ix.urz.uni-heidelberg.de

The Nup84p complex consists of five nucleoporins (Nup84p, Nup85p, Nup120p, Nup145p-C, and Seh1p) and Sec13p, a bona fide subunit of the COPII coat complex. We show that a pool of green fluorescent protein–tagged Sec13p localizes to the nuclear pores in vivo, and identify sec13 mutant alleles that are synthetically lethal with nup85{Delta} and affect the localization of a green fluorescent protein–Nup49p reporter protein. In the electron microscope, sec13 mutants exhibit structural defects in nuclear pore complex (NPC) and nuclear envelope organization. For the assembly of the complex, Nup85p, Nup120p, and Nup145p-C are essential. A highly purified Nup84p complex was isolated from yeast under native conditions and its molecular mass was determined to be 375 kD by quantitative scanning transmission electron microscopy and analytical ultracentrifugation, consistent with a monomeric complex. Furthermore, the Nup84p complex exhibits a Y-shaped, triskelion-like morphology 25 nm in diameter in the transmission electron microscope. Thus, the Nup84p complex constitutes a paradigm of an NPC structural module with distinct composition, structure, and a role in nuclear mRNA export and NPC bio- genesis.

Key Words: nuclear pore complex • nuclear envelope • Nup84p • Sec13p • electron microscopy

© 2000 The Rockefeller University Press

The present address of S. Siniossoglou and H. Santos-Rosa is Medical Research Council Laboratory of Molecular Biology, Division of Cell Biology, Hills Road, Cambridge CB2 2QH, UK.

Abbreviations used in this paper: GFP, green fluorescent protein; NPC, nuclear pore complex; ProtA, protein A; STEM, scanning transmission EM; TEV, tobacco etch virus; ts, temperature-sensitive.


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