title: Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.
abstract: Nuclear pore complexes (NPCs) are huge assemblies formed from ∼30 different nucleoporins, typically organized in subcomplexes. One module, the conserved Nup82 complex at the cytoplasmic face of NPCs, is crucial to terminate mRNA export. To gain insight into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted in yeast the Nup82-Nup159-Nsp1-Dyn2 complex, which was suitable for biochemical, biophysical, and electron microscopy analyses. Our integrative approach revealed that the yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of subunits. Based on all these data, we developed a three-dimensional structural model of the Nup82 complex that depicts how this module might be anchored to the NPC scaffold and concomitantly can interact with the soluble nucleocytoplasmic transport machinery.
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
authors: Monika
authors: M
authors: Gaik
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
authors: Dirk
authors: D
authors: Flemming
authors: Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
authors: Alexander
authors: A
authors: von Appen
authors: Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
authors: Panagiotis
authors: P
authors: Kastritis
authors: Division of Biophysics of Macromolecules, German Center Research Center, D-69120 Heidelberg, Germany.
authors: Norbert
authors: N
authors: Mücke
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
authors: Jessica
authors: J
authors: Fischer
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
authors: Philipp
authors: P
authors: Stelter
authors: Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
authors: Alessandro
authors: A
authors: Ori
authors: Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany.
authors: Khanh Huy
authors: KH
authors: Bui
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany.
authors: Jochen
authors: J
authors: Baßler
authors: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331.
authors: Elisar
authors: E
authors: Barbar
authors: Structural and Computational Biology Unit, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de martin.beck@embl.de.
authors: Martin
authors: M
authors: Beck
authors: Biochemistry Center of Heidelberg University, D-69120 Heidelberg, Germany ed.hurt@bzh.uni-heidelberg.de martin.beck@embl.de.
authors: Ed
authors: E
authors: Hurt
mesh_terms: D000595:Amino Acid Sequence; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D022022:Nuclear Pore / Q000648:ultrastructure*; D028861:Nuclear Pore Complex Proteins / Q000648:ultrastructure*; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D012441:Saccharomyces cerevisiae / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000648:ultrastructure*
chemical_list: C095897:NUP82 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; D029701:Saccharomyces cerevisiae Proteins
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