Evidence map›Paper›PMID 1508189›Full record

ArticleMolecular and cellular biology1992

NSR1 is required for pre-rRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits.

W C Lee, D Zabetakis, T Mélèse

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

69 citing papers in PubMed, 128 citations in OpenAlex.

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  18. Inositol pyrophosphates: structure, enzymology and function.Cellular and molecular life sciences : CMLS · 2009
    Review
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

W C LeeDepartment of Biological Sciences, Columbia University, New York, New York 10027.
D Zabetakis
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 GM44901-01
6 · The paper itself

Abstract

NSR1 is a yeast nuclear localization sequence-binding protein showing striking similarity in its domain structure to nucleolin. Cells lacking NSR1 are viable but have a severe growth defect. We show here that NSR1, like nucleolin, is involved in ribosome biogenesis. The nsr1 mutant is deficient in pre-rRNA processing such that the initial 35S pre-rRNA processing is blocked and 20S pre-rRNA is nearly absent. The reduced amount of 20S pre-rRNA leads to a shortage of 18S rRNA and is reflected in a change in the distribution of 60S and 40S ribosomal subunits; there is no free pool of 40S subunits, and the free pool of 60S subunits is greatly increased in size. The lack of free 40S subunits or the improper assembly of these subunits causes the nsr1 mutant to show sensitivity to the antibiotic paromomycin, which affects protein translation, at concentrations that do not affect the growth of the wild-type strain. Our data support the idea that NSR1 is involved in the proper assembly of pre-rRNA particles, possibly by bringing rRNA and ribosomal proteins together by virtue of its nuclear localization sequence-binding domain and multiple RNA recognition motifs. Alternatively, NSR1 may also act to regulate the nuclear entry of ribosomal proteins required for proper assembly of pre-rRNA particles.

Indexed as

Nuclear ProteinsRNA-Binding ProteinsRNA Processing, Post-TranscriptionalSaccharomyces cerevisiae ProteinsFungal ProteinsMutationParomomycinRibosomesRNA, RibosomalSaccharomyces cerevisiaeFungal ProteinsNSR1 protein, S cerevisiaeNuclear ProteinsParomomycinRNA-Binding ProteinsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID1508189
PMCPMC360260
OpenAlexW1950015906

What OpenQuestion holds

Textmetadata
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.