Evidence map›Paper›PMID 9271392›Full record

ArticleMolecular and cellular biology1997

SQT1, which encodes an essential WD domain protein of Saccharomyces cerevisiae, suppresses dominant-negative mutations of the ribosomal protein gene QSR1.

D P Eisinger, F A Dick, E Denke, B L Trumpower

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In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

41 citing papers in PubMed, 59 citations in OpenAlex.

  1. Trial
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  6. Review
  7. Eukaryotic Ribosome assembly and Nucleocytoplasmic Transport.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Review
  9. Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 inInternational journal of molecular sciences · 2019
    Article
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  12. Article
  13. Review
  14. Article
  15. Article
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  18. Article
  19. Sqt1p is an eight-bladed WD40 protein.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  20. Article
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

4 authors at 1 institution in 1 country.

D P EisingerDepartment of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.
F A Dick
E Denke
B L Trumpower
Dartmouth College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

QSR1 is an essential Saccharomyces cerevisiae gene, which encodes a 60S ribosomal subunit protein required for joining of 40S and 60S subunits. Truncations of QSR1 predicted to encode C-terminally truncated forms of Qsr1p do not substitute for QSR1 but do act as dominant negative mutations, inhibiting the growth of yeast when expressed from an inducible promoter. The dominant negative mutants exhibit a polysome profile characterized by 'half-mer' polysomes, indicative of a subunit joining defect like that seen in other qsr1 mutants (D. P. Eisinger, F. A. Dick, and B. L. Trumpower, Mol. Cell. Biol. 17:5136-5145, 1997.) By screening a high-copy yeast genomic library, we isolated several clones containing overlapping inserts of a novel gene that rescues the slow-growth phenotype of the dominant negative qsr1 truncations. The suppressor of qsr1 truncation mutants, SQT1, is an essential gene, which encodes a 47.1-kDa protein containing multiple WD repeats and which interacts strongly with Qsr1p in a yeast two-hybrid system. SQT1 restores growth and the "half-mer" polysome profile of the dominant negative qsr1 mutants to normal, but it does not rescue temperature-sensitive qsr1 mutants or the original qsr1-1 missense allele. In yeast cell lysates, Sqt1p fractionates as part of an oligomeric protein complex that is loosely associated with ribosomes but is distinct from known eukaryotic initiation factor complexes. Loss of SQT1 function by down regulation from an inducible promoter results in formation of half-mer polyribosomes and decreased Qsr1p levels on free 60S subunits. Sqt1p thus appears to be involved in a late step of 60S subunit assembly or modification in the cytoplasm.

Indexed as

Saccharomyces cerevisiae ProteinsSuppression, GeneticAmino Acid SequenceBinding SitesCytosolDNAFungal ProteinsGenes, FungalMolecular Sequence DataMutagenesisProtein BiosynthesisRibosomal ProteinsRibosomesSaccharomyces cerevisiaeDNAFungal ProteinsRibosomal ProteinsRPL10 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSQT1 protein, S cerevisiae

Identifiers

PMID9271392
PMCPMC232365
OpenAlexW2161759592

What OpenQuestion holds

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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.