ArticleMolecular biology of the cell1997
In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.bioRxiv : the preprint server for biology · 2026Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- The spatial network of skeletal proteins in a stony coral.Journal of the Royal Society, Interface · 2021Article
- Molecular and structural analysis of central transport channel in complex with Nup93 of nuclear pore complex.Protein science : a publication of the Protein Society · 2020Article
- Identification of the NovelG3 (Bethesda, Md.) · 2018Article
- Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Molecular & cellular proteomics : MCP · 2016Article
- Architecture of the fungal nuclear pore inner ring complex.Science (New York, N.Y.) · 2015Article
- Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel.Nature structural & molecular biology · 2015Article
- The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1.The Journal of cell biology · 2013Article
- FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties.The EMBO journal · 2009Article
- Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.The Journal of cell biology · 2007Article
- Article
- Nucleoporins NPP-1, NPP-3, NPP-4, NPP-11 and NPP-13 are required for proper spindle orientation in C. elegans.Developmental biology · 2006Article
- Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- In situ analysis of spatial relationships between proteins of the nuclear pore complex.Biophysical journal · 2002Article
- Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly.BMC genetics · 2002Article
- The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport.Molecular and cellular biology · 2001Article
- Multiple mechanisms of suppression circumvent transcription defects in an RNA polymerase mutant.Molecular and cellular biology · 2000Article
- The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import.Molecular biology of the cell · 2000Article
- Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.Molecular and cellular biology · 2000Article
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5 authors.
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Abstract
The yeast nucleoporins Nsp1p, Nup49p, and Nup57p form a complex at the nuclear pores which is involved in nucleocytoplasmic transport. To investigate the molecular basis underlying complex formation, recombinant full-length Nup49p and Nup57p and the carboxyl-terminal domain of Nsp1p, which lacks the FXFG repeat domain, were expressed in Escherichia coli. When the three purified proteins were mixed together, they spontaneously associated to form a 150-kDa complex of 1:1:1 stoichiometry. In this trimeric complex, Nup57p fulfills the role of an organizing center, to which Nup49p and Nsp1p individually bind. For this interaction to occur, only two heptad repeat regions of the Nsp1p carboxyl-terminal domain are required, each region being about 50 amino acids in length. Finally, the reconstituted complex has the capability to bind to full-length Nic96p but not to mutant forms which also do not interact in vivo. When added to permeabilized yeast cells, the complex associates with the nuclear envelope and the nuclear pores. We conclude that Nsp1p, Nup49p, and Nup57p can reconstitute a complex in vitro which is competent for further assembly with other components of nuclear pores.
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