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• W1515930873 abstract "Research Article3 January 1995free access Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p. P. Grandi P. Grandi EMBL, Heidelberg, Germany. Search for more papers by this author N. Schlaich N. Schlaich EMBL, Heidelberg, Germany. Search for more papers by this author H. Tekotte H. Tekotte EMBL, Heidelberg, Germany. Search for more papers by this author E.C. Hurt E.C. Hurt EMBL, Heidelberg, Germany. Search for more papers by this author P. Grandi P. Grandi EMBL, Heidelberg, Germany. Search for more papers by this author N. Schlaich N. Schlaich EMBL, Heidelberg, Germany. Search for more papers by this author H. Tekotte H. Tekotte EMBL, Heidelberg, Germany. Search for more papers by this author E.C. Hurt E.C. Hurt EMBL, Heidelberg, Germany. Search for more papers by this author Author Information P. Grandi1, N. Schlaich1, H. Tekotte1 and E.C. Hurt1 1EMBL, Heidelberg, Germany. The EMBO Journal (1995)14:76-87https://doi.org/10.1002/j.1460-2075.1995.tb06977.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Nic96p has been isolated previously in a complex together with the nuclear pore proteins Nsp1p, Nup49p and a p54 polypeptide. In a genetic screen for Nsp1p-interacting components, we now find NIC96, as well as a novel gene NUP57 which encodes the p54 protein (called Nup57p). Nup57p which is essential for cell growth contains GLFG repeats in the N-terminal half and heptad repeats in the C-terminal half. The domain organization of Nic96p is more complex: N-terminally located heptad repeats mediate binding to a trimeric Nsp1p-Nup49p-Nup57p complex, but are not required for the formation of this core complex; single amino acid substitutions in the central domain yield thermosensitive mutants, which do not impair interaction with the Nsp1 complex; the C-terminal domain is neither essential nor required for binding to the nucleoporin complex, but strikingly mutations in this part cause synthetic lethality with nsp1 and nup57 mutant alleles. Since a strain in which the Nic96p heptad repeats were deleted shows, similar to nsp1 and nup49 mutants, cytoplasmic mislocalization of a nuclear reporter protein, we propose that the interaction of the heterotrimeric Nsp1p-Nup49p-Nup57p core complex with Nic96p is required for protein transport into the nucleus. Previous ArticleNext Article Volume 14Issue 11 January 1995In this issue RelatedDetailsLoading ..." @default.
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• W1515930873 date "1995-01-01" @default.
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• W1515930873 title "Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p." @default.
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• W1515930873 doi "https://doi.org/10.1002/j.1460-2075.1995.tb06977.x" @default.
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