Evidence map›Paper›PMID 19129220›Full record

ArticleNucleic acids research2009

Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro.

Warawan Eiamphungporn, Sumarin Soonsanga, Jin-Won Lee, John D Helmann

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Positioning of extracellular loop 1 affects pore gating of the cystic fibrosis transmembrane conductance regulator.American journal of physiology. Lung cellular and molecular physiology · 2016
    Article
  3. Structure of the MarR family protein Rv0880 from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  4. Article
  5. Thiol-based redox switches.Biochimica et biophysica acta · 2014
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  11. Article
  12. Thiol-based redox switches and gene regulation.Antioxidants & redox signaling · 2011
    Review
  13. DNA-mediated charge transport in redox sensing and signaling.Journal of the American Chemical Society · 2010
    Article
  14. Article
  15. 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 2 institutions in 2 countries.

Warawan EiamphungpornDepartment of Microbiology, Cornell University, Ithaca, NY 14853-8101, USA.
Sumarin Soonsanga
Jin-Won Lee
John D Helmann
Cornell University · USHanyang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacillus subtilis OhrR is a dimeric repressor that senses organic peroxides and regulates the expression of the OhrA peroxiredoxin. Derepression results from oxidation of an active site cysteine which ultimately results in formation of a mixed disulfide with a low molecular weight thiol, a cyclic sulfenamide, or overoxidation to the sulfinic or sulfonic acids. We expressed a single-chain OhrR (scOhrR) in which the two monomers were connected by a short amino-acid linker. scOhrR variants containing only one active site cysteine were fully functional as repressors and still responded, albeit with reduced efficacy, to organic peroxides in vivo. Biochemical analyses indicate that oxidation at a single active site is sufficient for derepression regardless of the fate of the active site cysteine. scOhrR with only one active site cysteine in the amino-terminal domain is inactivated at rates comparable to wild-type whereas when the active site is in the carboxyl-terminal domain the protein is inactivated much more slowly. The incomplete derepression noted for single active site variants of scOhrR in vivo is consistent with the hypothesis that protein reduction regenerates active repressor and that, in the cell, oxidation of the second active site may also contribute to derepression.

Indexed as

Bacillus subtilisBacterial ProteinsBenzene DerivativesCysteineLinoleic AcidsLipid PeroxidesMutationOxidantsOxidation-ReductionPeroxidesRepressor ProteinsRNA, MessengerBacterial ProteinsBenzene Derivativescumene hydroperoxideCysteinelinoleic acid hydroperoxideLinoleic AcidsLipid PeroxidesOxidantsperoxide repressor proteinsPeroxidesRepressor ProteinsRNA, Messenger

Identifiers

PMID19129220
PMCPMC2651793
OpenAlexW2167196260

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.