Evidence map›Paper›PMID 19543924›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010

Interaction between cyanobacterial copper chaperone Atx1 and zinc homeostasis.

Samantha J Dainty, Carl J Patterson, Kevin J Waldron, Nigel J Robinson

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  4. Review
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  8. T versus D in the MTCXXC motif of copper transport proteins plays a role in directional metal transport.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  9. Article
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  11. Review
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  14. Crosstalk between Cu(I) and Zn(II) homeostasis via Atx1 and cognate domains.Chemical communications (Cambridge, England) · 2013
    Article
  15. Article
  16. Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Thermodynamics of copper and zinc distribution in the cyanobacterium Synechocystis PCC 6803.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. Review
  19. Article
  20. NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010
    Article
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.

Samantha J DaintyInstitute for Cell and Molecular Bioscience, Newcastle University, UK.
Carl J Patterson
Kevin J Waldron
Nigel J Robinson
Newcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E001688/1
6 · The paper itself

Abstract

Cyanobacterial Atx1 is a copper chaperone which interacts with two copper-transporting ATPases to assist copper supply to plastocyanin and cytochrome oxidase. ZiaA is a Zn(2+)-exporting ATPase and ziaA expression is regulated by ZiaR. Here we show that gene expression from the ziaA operator promoter, monitored using reverse transcriptase PCR and lacZ fusions, is elevated in Deltaatx1 mutants. Although Cu(+) tightly binds recombinant ZiaR in vitro, Cu(+) is less effective at dissociating ZiaR-DNA complexes than Zn(2+) and crucially ziaA expression responds to Zn(2+) but not copper in both wild-type and Deltaatx1 cells. Consistent with enhanced expression of ZiaA, Deltaatx1 cells have slightly elevated Zn(2+) resistance. Recombinant Zn(2+)-Atx1 is recovered from Zn(2+)-supplemented Escherichia coli and even after copper supplementation substantial amounts of Zn(2+)-Atx1 are isolated. Taken together, these data suggest that Zn(2+)-Atx1 can form in vivo.

Indexed as

HomeostasisAdenosine TriphosphatasesBacterial ProteinsCopperDNAEscherichia coliGene Expression Regulation, BacterialMolecular ChaperonesMutationPromoter Regions, GeneticSynechocystisZincAdenosine TriphosphatasesBacterial ProteinsCopperDNAMolecular ChaperonesZincZn(II)-translocating P-type ATPase

Identifiers

PMID19543924
OpenAlexW2134505561

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.