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PMID: 2112428 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain.

Cell ·Vol. 61 ·No. 6 ·1990-06-15 ·Pages 979-89

Nehrbass U, Kern H, Mutvei A, Horstmann H, Marshallsay B, Hurt EC

Abstract

NSP1 is located at the nuclear periphery in yeast and is essential for cell growth. Employing immunoelectron microscopy on yeast cells, we show that NSP1 is located at the nuclear pores. The molecular analysis of the NSP1 protein points to a two domain model: a nonessential domain (the first 603 amino acids) composed of repetitive sequences common to other nuclear proteins and an essential, carboxy-terminal domain (residues 604-823) mediating the vital function of NSP1. The NSP1 carboxy-terminal domain, which shows a heptad repeat organization, affected the correct location of two nuclear proteins: site-specific amino acid substitutions within a predicted alpha-helical structure of this domain caused a temperature-sensitive growth arrest at 37 degrees C and the appearance of NSP1 and NOP1, a nucleolar protein, in the cytosol.

MeSH Terms
Alcohol Dehydrogenase/genetics Amino Acid Sequence Calcium-Binding Proteins Chromosomes, Fungal Diploidy Fluorescent Antibody Technique Fungal Proteins/genetics,isolation & purification Genes, Fungal Haploidy Microscopy, Electron Molecular Sequence Data Mutation Nuclear Envelope/analysis,ultrastructure Nuclear Pore Complex Proteins Nuclear Proteins Polymerase Chain Reaction Promoter Regions, Genetic Protein Conformation Recombinant Fusion Proteins/isolation & purification Saccharomyces cerevisiae/cytology,growth & development,ultrastructure Saccharomyces cerevisiae Proteins Spores, Fungal/physiology Suppression, Genetic Temperature beta-Galactosidase/isolation & purification
Chemicals
Calcium-Binding Proteins Fungal Proteins NSP1 protein, S cerevisiae Nuclear Pore Complex Proteins Nuclear Proteins Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins Alcohol Dehydrogenase beta-Galactosidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Nehrbass U
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Kern H
Mutvei A
Horstmann H
Marshallsay B
Hurt E C
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1990-06-15
Pages
979-89
Language
English
Region
United States
NLM ID
0413066
Subset
IM
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