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PMID: 1464327 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.

The EMBO journal ·Vol. 11 ·No. 13 ·1992-12-00 ·Pages 5051-61

Wimmer C, Doye V, Grandi P, Nehrbass U, Hurt EC

Abstract

NSP1 is a nuclear pore protein (nucleoporin) essential for cell growth. To identify the components that functionally interact with NSP1 in the living cell, we developed a genetic screen for mutants that are lethal in a genetic background of mutated, but not wild type NSP1. Fourteen synthetic lethal mutants were obtained, belonging to at least four different complementation groups. The genes of two complementation groups, NSP116 and NSP49, were cloned. Like the previously described nucleoporins, these genes encode proteins with many repeat sequences. NSP116 and NSP49, however, contain a new repetitive sequence motif 'GLFG', which classifies them as a subclass of nucleoporins. NSP116 and NSP49, tagged with the IgG binding domain of protein A and expressed in yeast, are located at the nuclear envelope. These data provide in vivo evidence that distinct subclasses of nucleoporins physically interact or share overlapping function in nuclear pore complexes.

Related Genes
MeSH Terms
Amino Acid Sequence Base Sequence Calcium-Binding Proteins DNA, Fungal Fungal Proteins/genetics,metabolism Genetic Complementation Test Membrane Glycoproteins/classification,genetics,metabolism Molecular Sequence Data Nuclear Envelope/metabolism Nuclear Pore Complex Proteins Nuclear Proteins/classification,genetics,metabolism Plasmids Restriction Mapping Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Staphylococcal Protein A/metabolism
Chemicals
Calcium-Binding Proteins DNA, Fungal Fungal Proteins Membrane Glycoproteins NSP1 protein, S cerevisiae NUP116 protein, S cerevisiae NUP49 protein, S cerevisiae Nuclear Pore Complex Proteins Nuclear Proteins Saccharomyces cerevisiae Proteins Staphylococcal Protein A nuclear pore protein p62
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wimmer C
EMBL, Heidelberg, Germany.
Doye V
Grandi P
Nehrbass U
Hurt E C
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-12-00
Pages
5051-61
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556983
Subset
IM
Databases
GENBANK
D13199, D13200, D13201, D13202, D13203, M94783, M94784, M94785, X68108, X68109
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