Evidence map›Paper›PMID 7610056›Full record

ArticleNucleic acids research1995

Functional domains of the heavy metal-responsive transcription regulator MTF-1.

F Radtke, O Georgiev, H P Müller, E Brugnera, W Schaffner

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 1995. 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
3.1field-weighted citation impact, top 7% 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, 155 citations in OpenAlex.

  1. Review
  2. Article
  3. A T > G Mutation in theFrontiers in genetics · 2019
    Article
  4. Short-lived mammals (shrew, mouse) have a less robust metal-responsive transcription factor than humans and bats.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Nematode and snail metallothioneins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Review
  11. Characterization of MtnE, the fifth metallothionein member in Drosophila.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Nickel mobilizes intracellular zinc to induce metallothionein in human airway epithelial cells.American journal of respiratory cell and molecular biology · 2009
    Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

F RadtkeInstitut für Molekularbiologie II der Universität Zürich, Switzerland.
O Georgiev
H P Müller
E Brugnera
W Schaffner
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metallothioneins (MTs) constitute a class of low molecular weight, cysteine-rich, metal binding proteins which are regulated at the level of gene transcription in response to heavy metals and other adverse treatments. We have previously cloned a zinc finger factor (MTF-1) that binds specifically to heavy metal-responsive DNA sequence elements in metallothionein promoters and shown that this factor is essential for basal and heavy metal-induced transcription. Here we report that the C-terminal part of MTF-1 downstream of the DNA binding zinc fingers harbours three different transactivation domains, namely an acidic domain, a proline-rich domain and a domain rich in serine and threonine. When fused to the heterologous DNA binding domain of the yeast factor GAL4 these activation domains function constitutively, i.e. transcription of a GAL4-driven reporter gene is not induced by heavy metals. In search of the region(s) responsible for metal induction, external and internal deletion mutations of mouse and human MTF-1 and chimeric variants thereof were tested with a reporter gene driven by a metal-responsive promoter. The N-terminal part of MTF-1 containing the zinc fingers, which are dependent on zinc for efficient DNA binding, can indeed confer a limited (3- to 4-fold) zinc-responsive transcription when fused to the heterologous activation domain of the viral VP16 protein. Another region containing the acidic and proline-rich activation domains also contributes to metal inducibility, but only in the context of intact MTF-1. This indicates that the activity of MTF-1 results from a complex interplay of different functional domains.

Indexed as

Saccharomyces cerevisiae ProteinsBase SequenceBinding SitesDNADNA-Binding ProteinsFungal ProteinsGene DeletionHeLa CellsHerpes Simplex Virus Protein Vmw65HumansHydrogen-Ion ConcentrationMetallothioneinMetalsMolecular Sequence DataMutagenesisPlasmidsDNADNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeHerpes Simplex Virus Protein Vmw65MetallothioneinMetalsProlineRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSerineThreonineTranscription Factor MTF-1Transcription Factors

Identifiers

PMID7610056
PMCPMC307018
OpenAlexW2050443213

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.