Evidence map›Paper›PMID 8665859›Full record

ArticleThe EMBO journal1996

A heteromeric complex containing the centromere binding factor 1 and two basic leucine zipper factors, Met4 and Met28, mediates the transcription activation of yeast sulfur metabolism.

L Kuras, H Cherest, Y Surdin-Kerjan, D Thomas

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

73 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
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  7. Transcription Factor Condensates Mediate Clustering ofbioRxiv : the preprint server for biology · 2024
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  10. Mechanisms of Binding Specificity among bHLH Transcription Factors.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Homotypic cooperativity and collective binding are determinants of bHLH specificity and function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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.

L KurasCentre de Génétique Moleculaire, Centre National de la Recherche Scientifique, France.
H Cherest
Y Surdin-Kerjan
D Thomas
Centre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription activation of sulfur metabolism in yeast is dependent on two DNA binding factors, the centromere binding factor 1 (Cbf1) and Met4. While the role of Met4 was clearly established by showing that it acts as a transcription activator, the precise function in transcription of the multi-functional factor Cbf1 remains more elusive. We report here the identification of a new transcription factor Met28 which participates in the regulation of sulfur metabolism. Cloning and sequencing of MET28 revealed that it encodes a new member of the basic leucine zipper DNA binding factor family. We also demonstrate that Met28 possesses no intrinsic transcription activation capabilities. Studies of the DNA binding characteristics of Met28 led us to identify in gel mobility assays a heteromeric complex containing Cbf1, Met4 and Met28. We further demonstrated that the presence of Cbf1 and Met4 stimulates the binding of Met28 to DNA. 'Two-hybrid' studies allowed us to carry out preliminary investigations on the binary protein-protein interactions involved in the formation of the Cbf1-Met4-Met28 complex. Our results give evidence that the leucine zippers of Met4 and Met28, along with the basic helix-loop-helix domain of Cbf1, provide the protein surfaces mediating these interactions. All these results suggest that the multi-functional factor Cbf1 functions in transcription activation by tethering specific activating factors to the DNA.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBase SequenceBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBasic-Leucine Zipper Transcription FactorsBinding SitesCell LineDNA-Binding ProteinsFungal ProteinsHumansLeucine ZippersMacromolecular SubstancesMolecular Sequence DataSaccharomyces cerevisiaeSubstrate SpecificityBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBasic-Leucine Zipper Transcription FactorsCBF1 protein, S cerevisiaeDNA-Binding ProteinsFungal ProteinsMacromolecular SubstancesMET28 protein, S cerevisiaeMET4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSulfurTrans-ActivatorsTranscription Factors

Identifiers

PMID8665859
PMCPMC450184
OpenAlexW2268730793

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.