Evidence map›Paper›PMID 9159110›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor.

J A Graden, D R Winge

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 120 citations in OpenAlex.

  1. A Defense Strategy inMolecules (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Nonsense-mediated mRNA decay and metal ion homeostasis and detoxification in Saccharomyces cerevisiae.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
    Review
  9. Article
  10. Article
  11. Ceruloplasmin as a source of Cu for a fungal pathogen.Journal of inorganic biochemistry · 2021
    Article
  12. Article
  13. Article
  14. NADBiomolecules · 2020
    Review
  15. Cross-talk in NADCurrent genetics · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Metals in fungal virulence.FEMS microbiology reviews · 2018
    Review
  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

2 authors at 1 institution in 1 country.

J A GradenUniversity of Utah Health Sciences Center, Salt Lake City, UT 84132, USA.
D R Winge
University of Utah · US

Funding

METAL HOMEOSTATIC MECHANISMS IN YEASTR01CA061286 · NCI · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1994 to 2007
$1.6M
NCI NIH HHS CA 61286NCI NIH HHS R01 CA061286
6 · The paper itself

Abstract

The expression of a number of genes encoding products involved in copper ion uptake in yeast is specifically inhibited by copper ions. We show here that copper metalloregulation occurs through Cu-dependent repression of the transactivation activity of Mac1p. A segment of the yeast transcription factor Mac1p was identified that activated transcription in vivo in a heterologous system using fusion polypeptides with the yeast Gal4 DNA-binding domain. The Gal4/Mac1p hybrid exhibits transactivation activity that is repressed in cells cultured in the presence of copper salts and derepressed in cells with reduced copper uptake. The repressive effect is specific for copper ions. The concentration dependency of the Cu-inactivation of Gal4/Mac1p is similar to that of Cu-inhibition of CTR1 expression, a known Cu-regulated gene in vivo. Copper inhibition of gene expression is not observed with a Gal4/Mac1p chimera containing the MAC1(up1) substitution within the transactivation domain. Cells harboring the MAC1(up1) allele fail to attenuate FRE1 and CTR1 expression in a Cu-dependent manner. Additional MAC1(up) alleles exist within the first of two cysteine-rich sequence motifs adjacent to the His --> Gln MAC1(up1) encoded substitution. Thus, Cu-regulation of Mac1p function arises from a novel Cu-specific repression of the transactivation domain function. Models for the mechanism of Cu-repression of Mac1p function will be discussed.

Indexed as

Saccharomyces cerevisiae ProteinsTranscriptional ActivationAmino Acid Sequencebeta-GalactosidaseBinding SitesCobaltCopperCopper SulfateFungal ProteinsIronMolecular Sequence DataMutagenesis, Site-DirectedNickelNuclear ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaebeta-GalactosidaseCobaltCopperCopper SulfateFungal ProteinsIronMAC1 protein, S cerevisiaeNickelNuclear ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsZinc

Identifiers

PMID9159110
PMCPMC20816
OpenAlexW2076609405

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.