Evidence map›Paper›PMID 22715108›Full record

ArticlePlant physiology2012

The CopRS two-component system is responsible for resistance to copper in the cyanobacterium Synechocystis sp. PCC 6803.

Joaquín Giner-Lamia, Luis López-Maury, José C Reyes, Francisco J Florencio

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

45 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. From pond to platform: howJournal of bacteriology · 2026
    Review
  3. Article
  4. Review
  5. Regulatory Characterization of Two Cop Systems for Copper Resistance inInternational journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  16. Article
  17. Review
  18. A protease-mediated mechanism regulates the cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    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

4 authors at 2 institutions in 1 country.

Joaquín Giner-LamiaInstituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla, Consejo Superior de Investigaciones Científicas, E-41092 Seville, Spain.
Luis López-Maury
José C Reyes
Francisco J Florencio
Consejo Superior de Investigaciones Científicas · ESInstituto de Bioquímica Vegetal y Fotosíntesis · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic organisms need copper for cytochrome oxidase and for plastocyanin in the fundamental processes of respiration and photosynthesis. However, excess of free copper is detrimental inside the cells and therefore organisms have developed homeostatic mechanisms to tightly regulate its acquisition, sequestration, and efflux. Herein we show that the CopRS two-component system (also known as Hik31-Rre34) is essential for copper resistance in Synechocystis sp. PCC 6803. It regulates expression of a putative heavy-metal efflux-resistance nodulation and division type copper efflux system (encoded by copBAC) as well as its own expression (in the copMRS operon) in response to the presence of copper in the media. Mutants in this two-component system or the efflux system render cells more sensitive to the presence of copper in the media and accumulate more intracellular copper than the wild type. Furthermore, CopS periplasmic domain is able to bind copper, suggesting that CopS could be able to detect copper directly. Both operons (copMRS and copBAC) are also induced by the photosynthetic inhibitor 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone but this induction requires the presence of copper in the media. The reduced response of two mutant strains to copper, one lacking plastocyanin and a second one impaired in copper transport to the thylakoid, due to the absence of the P(I)-type ATPases PacS and CtaA, suggests that CopS can detect intracellular copper. In addition, a tagged version of CopS with a triple HA epitope localizes to both the plasma and the thylakoid membranes, suggesting that CopS could be involved in copper detection in both the periplasm and the thylakoid lumen.

Indexed as

Adaptation, PhysiologicalBacterial ProteinsBiological TransportCell MembraneCopperIntracellular SpaceModels, BiologicalOxidation-ReductionPeriplasmPlastocyaninPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryProtein TransportSignal TransductionSynechocystisBacterial ProteinsCopperPlastocyanin

Identifiers

PMID22715108
PMCPMC3425214
OpenAlexW2134687042

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.