Evidence map›Paper›PMID 8914516›Full record

ArticleMolecular & general genetics : MGG1996

Mutations in STS1 suppress the defect in 3' mRNA processing caused by the rna15-2 mutation in Saccharomyces cerevisiae.

N Amrani, M E Dufour, N Bonneaud, F Lacroute

Abstract read
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In one paragraph

Article in Molecular & general genetics : MGG, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

N AmraniCentre de Génétique Moléculaire du C.N.R.S., Laboratoire propre associé à I'Université Pierre et Marie Curie, Gif sur Yvette, France.
M E Dufour
N Bonneaud
F Lacroute
Sorbonne Université · FRCentre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a search for proteins associated with Rna15p in processing the 3' ends of messenger RNAs, we have looked for suppressors that correct, even partially, the thermosensitive growth defect of the rna15-2 mutant. Mutations in a single locus that we named SSM5, were able to suppress both the thermosensitivity of cell growth and the mRNA 3' processing defect associated with the rna15-2 mutation, but only slightly alleviated the thermosensitive growth defect of an rna14-1 mutant. The ssm5-1 mutant is sensitive to hydroxyurea at 37 degrees C, a drug that inhibits DNA synthesis. By screening for complementation of the hydroxyurea-sensitive phenotype we cloned the corresponding wild-type gene and found that it corresponds to the essential gene STS1 (also named DBF8). Sts1p has an apparent molecular weight of 30 kDa and was confirmed to be a cytosolic protein by immunofluorescence analysis. Western blot analysis indicates that the thermosensitive mutant strains rna15-2, rna14-1 and pap1-1 present a very low level of the Rna15p at 37 degrees C. The ssm5-1 mutation restores the level of Rna15p in the rna15-2 ssm5-1 double mutant. Use of the two-hybrid system suggests that Sts1p does not interact directly with Rna15p, but may be active as a homodimer. The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus.

Indexed as

Amino Acid Transport SystemsmRNA Cleavage and Polyadenylation FactorsMutationPolynucleotide AdenylyltransferaseRNA Processing, Post-TranscriptionalSaccharomyces cerevisiae ProteinsAllelesATP-Binding Cassette TransportersBase SequenceFungal ProteinsGene Expression Regulation, FungalGenes, SuppressorGenetic Complementation TestMembrane ProteinsMolecular Sequence DataNuclear ProteinsAmino Acid Transport SystemsATP-Binding Cassette TransportersBAP3 protein, S cerevisiaeFungal ProteinsMembrane ProteinsmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsPancreatitis-Associated ProteinsPAP1 protein, S cerevisiaePoly APolynucleotide AdenylyltransferaseREG3A protein, humanRNA14 protein, S cerevisiaeRNA15 protein, S cerevisiaeRNA, MessengerSaccharomyces cerevisiae ProteinsSTS1 protein, S cerevisiae

Identifiers

PMID8914516
OpenAlexW2020378226

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.