Evidence map›Paper›PMID 22451651›Full record

ArticleThe Journal of biological chemistry2012

Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR).

Srivatsa Dwarakanath, Amanda K Chaplin, Michael A Hough, Sébastien Rigali, Erik Vijgenboom, Jonathan A R Worrall

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Regulation of a nickel tolerance operon conserved inApplied and environmental microbiology · 2025
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  7. Review
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  9. Current issues in molecular biology · 2023
    Article
  10. Review
  11. Article
  12. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Complexation of the nickel and cobalt transcriptional regulator RcnR with DNA.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  17. Article
  18. Article
  19. Bacterial copper storage proteins.The Journal of biological chemistry · 2018
    Review
  20. 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

6 authors at 3 institutions in 3 countries.

Srivatsa DwarakanathSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, United Kingdom.
Amanda K ChaplinSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, United Kingdom.
Michael A HoughSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, United Kingdom.
Sébastien RigaliCentre for Protein Engineering, Institut de Chimie B6a, University of Liège, B-4000 Liège, Belgium.
Erik VijgenboomMolecular Biotechnology, Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, P. O. Box 9502, 2300RA Leiden, The Netherlands.
Jonathan A R WorrallSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, United Kingdom. Electronic address: jworrall@essex.ac.uk.
University of Essex · GBLeiden University · NLUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A copper-sensitive operon repressor protein (CsoR) has been identified in Streptomyces lividans (CsoR(Sl)) and found to regulate copper homeostasis with attomolar affinity for Cu(I). Solution studies reveal apo- and Cu(I)-CsoR(Sl) to be a tetramer assembly, and a 1.7-Å resolution crystal structure of apo-CsoR(Sl) reveals that a significant conformational change is necessary to enable Cu(I) binding. In silico prediction of the CsoR regulon was confirmed in vitro (EMSA) and in vivo (RNA-seq), which highlighted that next to the csoR gene itself, the regulon consists of two Cu(I) efflux systems involving a CopZ-like copper metallochaperone protein and a CopA P(1)-type ATPase. Although deletion of csoR has only minor effects on S. lividans development when grown under high copper concentrations, mutations of the Cu(I) ligands decrease tolerance to copper as a result of the Cu(I)-CsoR mutants failing to disengage from the DNA targets, thus inhibiting the derepression of the regulon. RNA-seq experiments carried out on samples incubated with exogenous copper and a ΔcsoR strain showed that the set of genes responding to copper stress is much wider than anticipated and largely extends beyond genes targeted by CsoR. This suggests more control levels are operating and directing other regulons in copper homeostasis beside the CsoR regulon.

Indexed as

Stress, PhysiologicalBacterial ProteinsCopperCrystallography, X-RayRegulonRepressor ProteinsStreptomyces lividansBacterial ProteinsCopA protein, BacteriaCopperRepressor Proteins

Identifiers

PMID22451651
PMCPMC3366776
OpenAlexW2058058850

What OpenQuestion holds

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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.