Evidence map›Paper›PMID 22198771›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.

Steve Tottey, Carl J Patterson, Lucia Banci, Ivano Bertini, Isabella C Felli, Anna Pavelkova, Samantha J Dainty, Rafael Pernil, Kevin J Waldron, Andrew W Foster and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
8.4field-weighted citation impact, top 2% 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, 97 citations in OpenAlex.

  1. AccA fromChemical science · 2026
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  8. A protease-mediated mechanism regulates the cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Review
  11. Physiological responses of three mono-species phototrophic biofilms exposed to copper and zinc.Environmental science and pollution research international · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Interplay between tolerance mechanisms to copper and acid stress inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Metal homeostasis and resistance in bacteria.Nature reviews. Microbiology · 2017
    Review
  17. Review
  18. 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

11 authors at 4 institutions in 3 countries.

Steve TotteyDepartment of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom.
Carl J Patterson
Lucia Banci
Ivano Bertini
Isabella C Felli
Anna Pavelkova
Samantha J Dainty
Rafael Pernil
Kevin J Waldron
Andrew W Foster
Nigel J Robinson
Durham University · GBInteruniversity Consortium for Magnetic Resonance · ITFraunhofer USA Center for Molecular Biotechnology · USNewcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E001688/1Biotechnology and Biological Sciences Research Council BB/H006052/1Biotechnology and Biological Sciences Research Council BB/H006052/2Biotechnology and Biological Sciences Research Council BB/H011110/1Biotechnology and Biological Sciences Research Council BBS/B/02576
6 · The paper itself

Abstract

Copper metallochaperones supply copper to cupro-proteins through copper-mediated protein-protein-interactions and it has been hypothesized that metallochaperones thereby inhibit copper from causing damage en route. Evidence is presented in support of this latter role for cyanobacterial metallochaperone, Atx1. In cyanobacteria Atx1 contributes towards the supply of copper to plastocyanin inside thylakoids but it is shown here that in copper-replete medium, copper can reach plastocyanin without Atx1. Unlike metallochaperone-independent copper-supply to superoxide dismutase in eukaryotes, glutathione is not essential for Atx1-independent supply to plastocyanin: Double mutants missing atx1 and gshB (encoding glutathione synthetase) accumulate the same number of atoms of copper per cell in the plastocyanin pool as wild type. Critically, Δatx1ΔgshB are hypersensitive to elevated copper relative to wild type cells and also relative to ΔgshB single mutants with evidence that hypersensitivity arises due to the mislocation of copper to sites for other metals including iron and zinc. The zinc site on the amino-terminal domain (ZiaA(N)) of the P(1)-type zinc-transporting ATPase is especially similar to the copper site of the Atx1 target PacS(N), and ZiaA(N) will bind Cu(I) more tightly than zinc. An NMR model of a substituted-ZiaA(N)-Cu(I)-Atx1 heterodimer has been generated making it possible to visualize a juxtaposition of residues surrounding the ZiaA(N) zinc site, including Asp(18), which normally repulse Atx1. Equivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of P(1)-type ATPases for metals other than Cu(I) is conserved, again consistent with a role for copper metallochaperones to withhold copper from binding sites for other metals.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCopperCulture MediaGlutathioneHomeostasisMetallochaperonesModels, MolecularMutationPlastocyaninProtein BindingSynechocystisZincAdenosine TriphosphatasesBacterial ProteinsCopperCulture MediaGlutathioneMetallochaperonesPlastocyaninZinc

Identifiers

PMID22198771
PMCPMC3252907
OpenAlexW2084123810

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.