Evidence map›Paper›PMID 9851990›Full record

ArticleJournal of bacteriology1998

Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.

B K Baxter, E A Craig

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  7. Recruitment of mRNA cleavage/polyadenylation machinery by the yeast chromatin protein Sin1p/Spt2p.Proceedings of the National Academy of Sciences of the United States of America · 2006
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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.

B K BaxterDepartment of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
E A Craig
University of Wisconsin–Madison · US

Funding

REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER37GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1999 to 2008
$3.3M
REGULATION AND FUNCTION OF THE YEAST HEAT SHOCK RESPONSER01GM031107 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 1985 to 2012
$1.9M
NIGMS NIH HHS GM31107NIGMS NIH HHS R01 GM031107NIGMS NIH HHS R37 GM031107
6 · The paper itself

Abstract

The Ssa subfamily of Hsp70 molecular chaperones in the budding yeast Saccharomyces cerevisiae has four members, encoded by SSA1, SSA2, SSA3, and SSA4. Deletion of the two constitutively expressed genes, SSA1 and SSA2, results in cells which are slow growing and temperature sensitive. In this study, we demonstrate that an extragenic suppressor of the temperature sensitivity of ssa1 ssa2 strains, EXA1-1, is a loss-of-function mutation in SIN1/SPT2, which encodes a nonhistone component of chromatin. Loss of function of Sin1p leads to overexpression of SSA3 in the ssa1 ssa2 mutant background, at a level which is sufficient to mediate suppression. In a strain which is wild type for SSA genes, we detected no effect of Sin1p on Ssa3p expression except under conditions of heat shock. Existing data indicate that expression of SSA3 in the ssa1 ssa2 mutant background as well as in heat-shocked wild-type strains is mediated by the heat shock transcription factor HSF. Our findings suggest that it is HSF-mediated induction of SSA3 which is modulated by Sin1p. The EXA1-1 suppressor mutation thus improves the growth of ssa1 ssa2 strains by selectively increasing HSF-mediated expression of SSA3.

Indexed as

MutagenesisSaccharomyces cerevisiae ProteinsSuppression, GeneticBacterial ProteinsChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene ExpressionHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPhenotypeSaccharomyces cerevisiaeBacterial ProteinsChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsSPT2 protein, S cerevisiaeSSA3 protein, S cerevisiaeStreptomyces trypsin inhibitor 1 protein, StreptomycesYDJ1 protein, S cerevisiae

Identifiers

PMID9851990
PMCPMC107749
OpenAlexW2148552953

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.