Evidence map›Paper›PMID 18687692›Full record

ArticleThe Journal of biological chemistry2008

Dual roles of an essential cysteine residue in activity of a redox-regulated bacterial transcriptional activator.

Nirupama Gupta, Stephen W Ragsdale

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. The transcriptional regulator CprK detects chlorination by combining direct and indirect readout mechanisms.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  4. The restricted metabolism of the obligate organohalide respiring bacterium Dehalobacter restrictus: lessons from tiered functional genomics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  5. Thiol-based redox switches and gene regulation.Antioxidants & redox signaling · 2011
    Review
  6. Review
  7. Article
  8. 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

2 authors at 1 institution in 1 country.

Nirupama GuptaDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Mighigan 48109-0606, USA.
Stephen W Ragsdale
University of Michigan–Ann Arbor · US

Funding

THE REDOX-MEDIATED REGULATION OF IRON-RESPONSIVE GENE EXPRESSION IN LIVERP20RR017675 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F · 2002 to 2011
$20.4M
NCRR NIH HHS 1P20RR17675
6 · The paper itself

Abstract

CprK from Desulfitobacterium dehalogenans is the first characterized transcriptional regulator of anaerobic dehalorespiration and is controlled at two levels: redox and effector binding. In the reduced state and in the presence of chlorinated aromatic compounds, CprK positively regulates expression of the cpr gene cluster. One of the products of the cpr gene cluster is CprA, which catalyzes the reductive dehalogenation of chlorinated aromatic compounds. Redox regulation of CprK occurs through a thiol/disulfide redox switch, which includes two classes of cysteine residues. Under oxidizing conditions, Cys11 and Cys200 form an intermolecular disulfide bond, whereas Cys105 and Cys111 form an intramolecular disulfide. Here, we report that Cys11 is involved in redox inactivation in vivo. Upon replacement of Cys11 with serine, alanine, or aspartate, CprK loses its DNA binding activity. C11A is unstable; however, circular dichroism studies demonstrate that the stability and overall secondary structures of CprK and the C11S and C11D variants are similar. Furthermore, effector binding remains intact in the C11S and C11D variants. However, fluorescence spectroscopic results reveal that the tertiary structures of the C11S and C11D variants differ from that of the wild type protein. Thus, Cys11 plays a dual role as a redox switch and in maintaining the correct tertiary structure that promotes DNA binding.

Indexed as

Oxidation-ReductionTranscriptional ActivationBacterial ProteinsCloning, MolecularCysteineDisulfidesDNAGenes, ReporterMass SpectrometryModels, BiologicalModels, MolecularMolecular ConformationMutagenesis, Site-DirectedOxygenSpectrometry, FluorescenceTranscription FactorsBacterial ProteinsCysteineDisulfidesDNAOxygenTranscription Factors

Identifiers

PMID18687692
PMCPMC2568902
OpenAlexW1986362483

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.