Evidence map›Paper›PMID 19965775›Full record

ArticleNucleic acids research2010

The CCAAT-binding complex coordinates the oxidative stress response in eukaryotes.

Marcel Thön, Qusai Al Abdallah, Peter Hortschansky, Daniel H Scharf, Martin Eisendle, Hubertus Haas, Axel A Brakhage

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.2field-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

51 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Oxidative stress response pathways in fungi.Cellular and molecular life sciences : CMLS · 2022
    Review
  7. Article
  8. Increasing NADPH impairs fungal HBioresources and bioprocessing · 2022
    Article
  9. Article
  10. Article
  11. Article
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  15. Article
  16. Review
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  18. Genome-wide identification and co-expression network analysis of nuclear factor-Y in barley revealed potential functions in salt stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2019
    Article
  19. Article
  20. Review
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

7 authors at 4 institutions in 3 countries.

Marcel ThönDepartment of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Beutenbergstrasse 11a, D-07745 Jena, Germany.
Qusai Al Abdallah
Peter Hortschansky
Daniel H Scharf
Martin Eisendle
Hubertus Haas
Axel A Brakhage
Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DEBiocenter Finland · FIFriedrich Schiller University Jena · DEInnsbruck Medical University · AT

Funding

Austrian Science Fund FWF P 18606
6 · The paper itself

Abstract

The heterotrimeric CCAAT-binding complex is evolutionary conserved in eukaryotic organisms. The corresponding Aspergillus nidulans CCAAT-binding factor (AnCF) consists of the subunits HapB, HapC and HapE. All of the three subunits are necessary for DNA binding. Here, we demonstrate that AnCF senses the redox status of the cell via oxidative modification of thiol groups within the histone fold motif of HapC. Mutational and in vitro interaction analyses revealed that two of these cysteine residues are indispensable for stable HapC/HapE subcomplex formation and high-affinity DNA binding of AnCF. Oxidized HapC is unable to participate in AnCF assembly and localizes in the cytoplasm, but can be recycled by the thioredoxin system in vitro and in vivo. Furthermore, deletion of the hapC gene led to an impaired oxidative stress response. Therefore, the central transcription factor AnCF is regulated at the post-transcriptional level by the redox status of the cell serving for a coordinated activation and deactivation of antioxidative defense mechanisms including the specific transcriptional activator NapA, production of enzymes such as catalase, thioredoxin or peroxiredoxin, and maintenance of a distinct glutathione homeostasis. The underlying fine-tuned mechanism very likely represents a general feature of the CCAAT-binding complexes in eukaryotes.

Indexed as

Gene Expression Regulation, FungalOxidative StressActive Transport, Cell NucleusAspergillus nidulansCCAAT-Binding FactorCell NucleusCysteineDimerizationDNAFungal ProteinsGene DeletionOxidation-ReductionPromoter Regions, GeneticProteomeThioredoxin-Disulfide ReductaseThioredoxinsaab-1 protein, NeurosporaAnCF protein, Aspergillus nidulansCCAAT-Binding FactorCysteineDNAFungal ProteinsProteomeThioredoxin-Disulfide ReductaseThioredoxins

Identifiers

PMID19965775
PMCPMC2831313
OpenAlexW2163358830

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.