The NUP1 gene encodes an essential component of the yeast nuclear pore complex

Davis, Laura I.; Fink, Gerald R.

doi:10.1016/0092-8674(90)90062-j

Cited by 216 publications

(211 citation statements)

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“…When epitope tagged, Rat3p was localized to the nuclear rim in a pattern identical to that of the Ags recognized by the antinucleoporin antibody RL1. A similar punctate nuclear rim staining pattern has been seen for all yeast NPC proteins whose localization has been examined (Davis and Fink, 1990;Nehrbass et al, 1990;Wimmer et al, 1992;Yano et al, 1992;Loeb et al, 1993;Fabre et al, 1994;Wente and Blobel, 1994;Wozniak et al, 1994) and has only been seen for nuclear pore proteins. Combinations of mutant alleles of nucleoporins are often lethal (synthetic lethality) (Wimmer et al, 1992;Loeb et al, 1993;Belanger et al, 1994;Wente and Blobel, 1994).…”

Section: Discussionmentioning

confidence: 70%

“…Most of these nucleoporins are characterized by the presence of unique repeat motifs that are present in 12-30 copies. Nuplp (Davis and Fink, 1990), Nup2p (Loeb et al, 1993), and Nsplp (Nehrbass et al, 1990) are members of the XFXFG-repeat-containing family. A second group of yeast nucleoporins that includes Nup49p, NuplOOp, Nupll6p (Wente et al, 1992;Wimmer et al, 1992;Wente and Blobel, 1994), and Nupl45p (Fabre et al, 1994;Wente and Blobel, 1994) have repeats of GLFG in their N-terminal and central domains.…”

Section: Discussionmentioning

confidence: 99%

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Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.

Heath

Amberg

et al. 1995

MBoC

119

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To identify genes whose products play potential roles in the nucleocytoplasmic export of messenger RNA, we isolated temperature-sensitive strains of Saccharomyces cerevisiae and examined them by fluorescent in situ hybridization. With the use of a digoxigen-tagged oligo-(dT)50 probe, we identified those that showed nuclear accumulation of poly(A)+ RNA when cells were shifted to the nonpermissive temperature. We describe here the properties of yeast strains bearing the rat3-1 mutation (RAT -ribonucleic acid trafficking) and the cloning of the RAT3 gene. When cultured at the permissive temperature of 23°C, fewer than 10% of cells carrying the rat3-1 allele showed nuclear accumulation of poly(A)+ RNA, whereas approximately 70% showed nuclear accumulation of poly(A)+ RNA after a shift to 37°C for 4 h. In wild-type cells, nuclear pore complexes (NPCs) are distributed relatively evenly around the nuclear envelope. Both indirect immunofluorescence analysis and electron microscopy of rat3-1 cells indicated that NPCs were clustered into one or a few regions of the NE in mutant cells. Similar NPC clustering was seen in mutant cells cultured at temperatures between 15°C and 37°C. The RAT3 gene encodes an 1157-amino acid protein without similarity to other known proteins. It is essential for growth only at 37°C. Cells carrying a disruption of the RAT3 gene were very similar to cells carrying the original rat3-1 mutation; they showed temperature-dependent nuclear accumulation of poly(A)+ RNA and exhibited constitutive clustering of NPCs. Epitope tagging of Rat3p demonstrated that it is located at the nuclear periphery and co-localizes with nuclear pore proteins recognized by the RL1 monoclonal antibody. We refer to this nucleoporin as Rat3p/Nupl33p.

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Section: Discussionmentioning

confidence: 70%

Section: Discussionmentioning

confidence: 99%

Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.

Heath

Amberg

et al. 1995

MBoC

119

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“…At short fixation times, the Gle2p-HA was concentrated in a punctate pattern at the nuclear periphery (Figure 3). This is typical of yeast nuclear pore complexes (Davis and Fink, 1990 (Figure 4) with samples of both total yeast cell lysate and enriched NPCs was divided in half and probed with either the anti-Gle2p antibody or an affinitypurified polyclonal antibody recognizing Nupil6p (Iovine et al, 1995). Gle2p migrated with an apparent molecular mass of 40 kDa and was present in the enriched NPC fraction.…”

Section: Gle2p Is Associated With Npcsmentioning

confidence: 99%

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

Murphy

Watkins

Wente

1996

MBoC

168

164

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To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin NuplOOp were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srplp, the nuclear localization signal receptor, as well as Riplp, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.

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“…Among these were the pore proteins NUPl [48], NUP2 [52], NUP49, NUPlOO and NUPl16 [53]. Besides, the nuclear pore protein NSPl [47] was identified in yeast by raising antibodies against the insoluble nuclear fraction [54].…”

Section: Isolation Of Nuclear Pores and Pore Componentsmentioning

confidence: 99%

“…P62 can be divided into three parts consisting of a N-terminal domain with 12 repeats similar to those found in the yeast pore proteins NSPI [47] and NUPl [48], an adjacent Ser/Thr rich sequence followed by a unique carboxy-terminal domain which is organized into amphiphilic heptad repeats with the potential to form coiled-coil interaction.…”

Section: Isolation Of Nuclear Pores and Pore Componentsmentioning

confidence: 99%

The nuclear pore complex

Hurt

1993

FEBS Letters

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Over the past years, significant progress has been made both in the analysis of the structural and molecular organization of the nuclear pore complex (NPC) and the mechanism of nuclear transport. In this minireview, I will focus on some of the recent developments in this field. Structural studies employing high resolution EM have revealed a detailed view of the three-dimensional organization of the NPC. In addition, an isolation procedure which yields highly enriched NPCs from yeast has given insight into the molecular complexity of the NPC organization. By biochemical, immunological and genetic approaches, a series of novel pore proteins were identified. Exploiting yeast as a genetic system, several mutants defective in nuclear import of proteins and export of RNA were selected. By in vitro nuclear transport assays, soluble cytoplasmic factors including NLS (nuclear localization sequence) binding proteins and heat shock proteins required for nuclear accumulation were found. The aim of the future research must be to put these various components of the NPC and nuclear transport machinery in a topological and functional context. Nuclear pore; Nuclear pore complex; Nuclear transport; Nuclear envelope; Nuclear localization sequence; Nucleoporin GENERAL OVERVIEWThe nucleus is surrounded by a double membrane which compartmentalizes nuclear and cytoplasmic reactions. Besides its key role in regulating nucleocytoplasmic transport, the nuclear membrane provides a structural support for the attachment of other macromolecular structures such as the nuclear lamina, nucleoskeleton, cytoskeleton and chromatin. Furthermore, the outer nuclear membrane, which is covered with ribosomes and continuous with the ER, is a site for protein synthesis and protein translocation.The transport of molecules and macromolecules across the nuclear membrane occurs through the nuclear pore complexes (NPCs). Several aspects of both the structural organization of the NPC and its role in nuclear transport reactions have been reviewed extensively [l-lo]. It has been estimated that up to one hundred proteins constitute the NPC. How these proteins are involved in the biogenesis and structural organization of the nuclear pore complex and in nucleocytoplasmic trafficking remains a challenging question for the next decade of research.For molecules to enter the cell nucleus, two mechanisms exist: passive diffusion of small molecules, and active transport of large macromolecules. The exclusion limit for diffusion is approximately 40-60 kDa [l 11. If large molecules have to enter the nucleus, they require active transport which is ATP and temperature depend- 76 ent [12]. However, even small and diffusable nuclear proteins such as histone Hl are actively imported into the nucleus [13,14].Targeting sequences on nuclear proteins are responsible for specific organelle sorting. One of the first nuclear targeting signals (NLS = nuclear localization sequence) to be identified was the short, 7 amino acid long sequence Pro-Lys-Lys-Lys-Arg-Lys-Val (PKKKRKV) of SV40 l...

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The NUP1 gene encodes an essential component of the yeast nuclear pore complex

Cited by 216 publications

References 50 publications

Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.

Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

The nuclear pore complex

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