Evidence map›Paper›PMID 9858564›Full record

ArticleMolecular and cellular biology1999

A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress.

K A Morano, N Santoro, K A Koch, D J Thiele

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  3. Article
  4. Genetic inactivation of essentialMolecular biology of the cell · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Review
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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 1 institution in 1 country.

K A MoranoDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0606, USA.
N Santoro
K A Koch
D J Thiele
University of Michigan–Ann Arbor · US

Funding

Training Program in Tumor MicroenvironmentT32CA009676 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Maria G Castro, Analisa Virginia DiFeo · 1992 to 2026
$7.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
HEAT SHOCK FACTOR--STRESS AND THE CELL CYCLEF32GM019195 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORANO, KEVIN A · 1998 to 1999
–
NCI NIH HHS 5T32CA09676-06NCI NIH HHS T32 CA009676NIGMS NIH HHS 1F32 GM19195-01NIGMS NIH HHS F32 GM019195NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Gene expression in response to heat shock is mediated by the heat shock transcription factor (HSF), which in yeast harbors both amino- and carboxyl-terminal transcriptional activation domains. Yeast cells bearing a truncated form of HSF in which the carboxyl-terminal transcriptional activation domain has been deleted [HSF(1-583)] are temperature sensitive for growth at 37 degreesC, demonstrating a requirement for this domain for sustained viability during thermal stress. Here we demonstrate that HSF(1-583) cells undergo reversible cell cycle arrest at 37 degreesC in the G2/M phase of the cell cycle and exhibit marked reduction in levels of the molecular chaperone Hsp90. As in higher eukaryotes, yeast possesses two nearly identical isoforms of Hsp90: one constitutively expressed and one highly heat inducible. When expressed at physiological levels in HSF(1-583) cells, the inducible Hsp90 isoform encoded by HSP82 more efficiently suppressed the temperature sensitivity of this strain than the constitutively expressed gene HSC82, suggesting that different functional roles may exist for these chaperones. Consistent with a defect in Hsp90 production, HSF(1-583) cells also exhibited hypersensitivity to the Hsp90-binding ansamycin antibiotic geldanamycin. Depletion of Hsp90 from yeast cells wild type for HSF results in cell cycle arrest in both G1/S and G2/M phases, suggesting a complex requirement for chaperone function in mitotic division during stress.

Indexed as

Saccharomyces cerevisiae ProteinsTranscriptional ActivationAntibiotics, AntineoplasticBenzoquinonesCell CycleDNA-Binding ProteinsFungal ProteinsGenes, FungalHeat-Shock ProteinsHeat-Shock ResponseHSP90 Heat-Shock ProteinsLactams, MacrocyclicQuinonesSaccharomyces cerevisiaeStructure-Activity RelationshipTemperatureAntibiotics, AntineoplasticBenzoquinonesDNA-Binding ProteinsFungal ProteinsgeldanamycinHeat-Shock ProteinsHSF1 protein, S cerevisiaeHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsLactams, MacrocyclicQuinonesSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID9858564
PMCPMC83898
OpenAlexW2132585346

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.