Evidence map›Paper›PMID 24831014›Full record

ArticleThe Journal of biological chemistry2014

Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR).

Feng-Ming James Chang, H Jerome Coyne, Ciro Cubillas, Pablo Vinuesa, Xianyang Fang, Zhen Ma, Dejian Ma, John D Helmann, Alejandro García-de los Santos, Yun-Xing Wang and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 65 citations in OpenAlex.

  1. Regulation of a nickel tolerance operon conserved inApplied and environmental microbiology · 2025
    Article
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  3. Compatibility of intracellular binding: Evolutionary design principles for metal sensors.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  13. HThe Journal of biological chemistry · 2020
    Review
  14. Review
  15. Functional Prediction and Assignment ofFrontiers in genetics · 2020
    Article
  16. Complexation of the nickel and cobalt transcriptional regulator RcnR with DNA.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  17. Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018
    Article
  18. Article
  19. Article
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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

12 authors at 4 institutions in 2 countries.

Feng-Ming James ChangFrom the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102.
H Jerome CoyneFrom the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102.
Ciro Cubillasthe Programa de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Apdo. Postal 565-A, Cuernavaca, Morelos, México, 04510.
Pablo Vinuesathe Programa de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Apdo. Postal 565-A, Cuernavaca, Morelos, México, 04510.
Xianyang Fangthe Structural Biophysics Laboratory, Center for Cancer Research, NCI-National Institutes of Health, Frederick, Maryland 21702-1201, and.
Zhen Mathe Department of Microbiology, Cornell University, Ithaca, New York 14853-8101.
Dejian MaFrom the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102.
John D Helmannthe Department of Microbiology, Cornell University, Ithaca, New York 14853-8101.
Alejandro García-de los Santosthe Programa de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Apdo. Postal 565-A, Cuernavaca, Morelos, México, 04510.
Yun-Xing Wangthe Structural Biophysics Laboratory, Center for Cancer Research, NCI-National Institutes of Health, Frederick, Maryland 21702-1201, and.
Charles E DannFrom the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102.
David P GiedrocFrom the Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102, giedroc@indiana.edu.
Indiana University Bloomington · USUniversidad Nacional Autónoma de México · MXCornell University · USNational Institutes of Health · US

Funding

SAXS FacilityZICBC011535 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WANG, YUN XING M · 2014 to 2025
$7.5M
ZINC COORDINATION AND REGULATION OF ZINC METALLOPROTEINSR01GM042569 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 1996 to 2015
$4.9M
ZINC DOMAIN STRUCTURE AND FUNCTION IN T4 GENE 32 PROTEINR29GM042569 · NIGMS · TEXAS AGRILIFE RESEARCH · PI GIEDROC, DAVID P. · 1991 to 1995
–
NIGMS NIH HHS GM042569NIGMS NIH HHS R01 GM042569
6 · The paper itself

Abstract

The copper-sensing operon repressor (CsoR) is representative of a major Cu(I)-sensing family of bacterial metalloregulatory proteins that has evolved to prevent cytoplasmic copper toxicity. It is unknown how Cu(I) binding to tetrameric CsoRs mediates transcriptional derepression of copper resistance genes. A phylogenetic analysis of 227 DUF156 protein members, including biochemically or structurally characterized CsoR/RcnR repressors, reveals that Geobacillus thermodenitrificans (Gt) CsoR characterized here is representative of CsoRs from pathogenic bacilli Listeria monocytogenes and Bacillus anthracis. The 2.56 Å structure of Cu(I)-bound Gt CsoR reveals that Cu(I) binding induces a kink in the α2-helix between two conserved copper-ligating residues and folds an N-terminal tail (residues 12-19) over the Cu(I) binding site. NMR studies of Gt CsoR reveal that this tail is flexible in the apo-state with these dynamics quenched upon Cu(I) binding. Small angle x-ray scattering experiments on an N-terminally truncated Gt CsoR (Δ2-10) reveal that the Cu(I)-bound tetramer is hydrodynamically more compact than is the apo-state. The implications of these findings for the allosteric mechanisms of other CsoR/RcnR repressors are discussed.

Indexed as

Allosteric RegulationBacillus anthracisBacterial ProteinsCopperDNA, BacterialGene Expression Regulation, BacterialGeobacillusModels, MolecularOperonPhylogenyProtein MultimerizationProtein Structure, QuaternaryRepressor ProteinsTranscription, GeneticBacterial ProteinsCopperDNA, BacterialRepressor ProteinsCopperMetalloregulationMetal Sensor ProteinPhylogeneticsTranscription RepressorX-ray CrystallographyX-ray Scattering

Identifiers

PMID24831014
PMCPMC4081955
OpenAlexW2061801760

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.