Evidence map›Paper›PMID 8245119›Full record

ArticleThe Journal of cell biology1993

Multiple regions of NSR1 are sufficient for accumulation of a fusion protein within the nucleolus.

C Yan, T Mélèse

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 61 citations in OpenAlex.

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  6. Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event.Proceedings of the National Academy of Sciences of the United States of America · 2007
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  18. Ultraviolet-induced movement of the human DNA repair protein, Xeroderma pigmentosum type G, in the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

C YanDepartment of Biological Sciences, Columbia University, New York 10027.
T Mélèse
Columbia University · US

Funding

BIOCHEMICAL AND GENETIC ANALYSIS OF NUCLEAR TRANSPORTR01GM044901 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MELESE, TERI · 1991 to 1995
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NUCLEAR PORE COMPLEX STRUCTURE/FUNCTIONR21GM044901 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MELESE, TERI · 1997 to 1998
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NIGMS NIH HHS GM-44901-01
6 · The paper itself

Abstract

NSR1, a 67-kD nucleolar protein, was originally identified in our laboratory as a nuclear localization signal binding protein, and has subsequently been found to be involved in ribosome biogenesis. NSR1 has three regions: an acidic/serine-rich NH2 terminus, two RNA recognition motifs, and a glycine/arginine-rich COOH terminus. In this study we show that NSR1 itself has a bipartite nuclear localization sequence. Deletion of either basic amino acid stretch results in the mislocation of NSR1 to the cytoplasm. We further demonstrate that either of two regions, the NH2 terminus or both RNA recognition motifs, are sufficient to localize a bacterial protein, beta-galactosidase, to the nucleolus. Intensive deletion analysis has further defined a specific acidic/serine-rich region within the NH2 terminus as necessary for nucleolar accumulation rather than nucleolar targeting. In addition, deletion of either RNA recognition motif or point mutations in one of the RNP consensus octamers results in the mislocalization of a fusion protein within the nucleus. Although the glycine/arginine-rich region in the COOH terminus is not sufficient to bring beta-galactosidase to the nucleolus, our studies show that this domain is necessary for nucleolar accumulation when an RNP consensus octamer in one of the RNA recognition motifs is mutated. Our findings are consistent with the notion that nucleolar localization is a result of the binding interactions of various domains of NSR1 within the nucleolus rather than the presence of a specific nucleolar targeting signal.

Indexed as

Nuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceBiological TransportCell FractionationCell NucleolusCell NucleusDNA Mutational AnalysisFluorescent Antibody TechniqueFungal ProteinsGenes, ReporterMolecular Sequence DataPromoter Regions, GeneticProtein Sorting SignalsFungal ProteinsNSR1 protein, S cerevisiaeNuclear ProteinsProtein Sorting SignalsRecombinant Fusion ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID8245119
PMCPMC2119886
OpenAlexW2146024983

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.