Evidence map›Paper›PMID 21445264›Full record

ArticlePloS one2011

The cyanobacterial hepatotoxin microcystin binds to proteins and increases the fitness of microcystis under oxidative stress conditions.

Yvonne Zilliges, Jan-Christoph Kehr, Sven Meissner, Keishi Ishida, Stefan Mikkat, Martin Hagemann, Aaron Kaplan, Thomas Börner, Elke Dittmann

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed
19.2field-weighted citation impact, top 1% 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

143 citing papers in PubMed, 448 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Secondary metabolism ofApplied and environmental microbiology · 2026
    Review
  5. Article
  6. Article
  7. Cyanobacteria Under UV Radiation: General Insights into Stress Responses.International journal of molecular sciences · 2025
    Review
  8. Tracking putativemSystems · 2025
    Article
  9. Impact of high temperature and UVR exposure on the microcystin production and mcyB gene expression in the cyanobacterium Microcystis aeruginosa.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  10. Article
  11. Article
  12. Differential impact of microcystins MC-LR and [D-LeuCurrent research in microbial sciences · 2025
    Article
  13. ISME communications · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Microbiome analysis revealsApplied and environmental microbiology · 2024
    Article
  19. Article
  20. Closed circular genome sequence of aMicrobiology resource announcements · 2023
    Article

83 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

9 authors at 5 institutions in 2 countries.

Yvonne ZilligesInstitute of Biology, Department of Molecular Ecology, Humboldt University, Berlin, Germany.
Jan-Christoph Kehr
Sven Meissner
Keishi Ishida
Stefan Mikkat
Martin Hagemann
Aaron Kaplan
Thomas Börner
Elke Dittmann
University of Potsdam · DEHumboldt-Universität zu Berlin · DEUniversity of Rostock · DEHebrew University of Jerusalem · ILLeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microcystins are cyanobacterial toxins that represent a serious threat to drinking water and recreational lakes worldwide. Here, we show that microcystin fulfils an important function within cells of its natural producer Microcystis. The microcystin deficient mutant ΔmcyB showed significant changes in the accumulation of proteins, including several enzymes of the Calvin cycle, phycobiliproteins and two NADPH-dependent reductases. We have discovered that microcystin binds to a number of these proteins in vivo and that the binding is strongly enhanced under high light and oxidative stress conditions. The nature of this binding was studied using extracts of a microcystin-deficient mutant in vitro. The data obtained provided clear evidence for a covalent interaction of the toxin with cysteine residues of proteins. A detailed investigation of one of the binding partners, the large subunit of RubisCO showed a lower susceptibility to proteases in the presence of microcystin in the wild type. Finally, the mutant defective in microcystin production exhibited a clearly increased sensitivity under high light conditions and after hydrogen peroxide treatment. Taken together, our data suggest a protein-modulating role for microcystin within the producing cell, which represents a new addition to the catalogue of functions that have been discussed for microbial secondary metabolites.

Indexed as

Oxidative StressLightMicrocystinsMicrocystisOxidation-ReductionProtein BindingRibulose-Bisphosphate CarboxylasemicrocystinMicrocystinsRibulose-Bisphosphate Carboxylase

Identifiers

PMID21445264
PMCPMC3060824
OpenAlexW1990839717

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.