Evidence map›Paper›PMID 22992749›Full record

ArticleThe Journal of biological chemistry2012

The oxidation-sensing regulator (MosR) is a new redox-dependent transcription factor in Mycobacterium tuberculosis.

Pedro Brugarolas, Farahnaz Movahedzadeh, Yuehong Wang, Nan Zhang, Iona L Bartek, Yihe N Gao, Martin I Voskuil, Scott G Franzblau, Chuan He

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
2.7field-weighted citation impact, top 10% 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, 86 citations in OpenAlex.

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  2. Inorganic sulfate is critical forProceedings of the National Academy of Sciences of the United States of America · 2025
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  14. A novel stress-inducible CmtR-ESX3-ZnThe Journal of biological chemistry · 2020
    Article
  15. Review
  16. Article
  17. MarR Family Transcription Factors fromMicrobiology and molecular biology reviews : MMBR · 2019
    Review
  18. Article
  19. 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

9 authors at 3 institutions in 1 country.

Pedro BrugarolasDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA.
Farahnaz Movahedzadeh
Yuehong Wang
Nan Zhang
Iona L Bartek
Yihe N Gao
Martin I Voskuil
Scott G Franzblau
Chuan He
University of Illinois Chicago · USUniversity of Chicago · USUniversity of Colorado Denver · US

Funding

Tuning Virulence Determinants in Staphylococcus aureusR01AI074658 · NIAID · UNIVERSITY OF CHICAGO · PI HE, CHUAN · 2007 to 2016
$3.8M
The Mycobacterium Tuberculosis Dormancy ProgramR01AI061505 · NIAID · UNIVERSITY OF COLORADO DENVER · PI VOSKUIL, MARTIN INUA · 2005 to 2015
$3.6M
Re-Engineering Translational Research at the University of ChicagoTL1TR000432 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$289k
NCATS NIH HHS TL1 TR000432NIAID NIH HHS AI074658NIAID NIH HHS R01 AI061505NIAID NIH HHS R01 AI074658
6 · The paper itself

Abstract

Mycobacterium tuberculosis thrives in oxidative environments such as the macrophage. To survive, the bacterium must sense and adapt to the oxidative conditions. Several antioxidant defenses including a thick cell wall, millimolar concentrations of small molecule thiols, and protective enzymes are known to help the bacterium withstand the oxidative stress. However, oxidation-sensing regulators that control these defenses have remained elusive. In this study, we report a new oxidation-sensing regulator, Rv1049 or MosR (M. tuberculosis oxidation-sensing regulator). MosR is a transcriptional repressor of the MarR family, which, similarly to Bacillus subtilis OhrR and Staphylococcus aureus MgrA, dissociates from DNA in the presence of oxidants, enabling transcription. MosR senses oxidation through a pair of cysteines near the N terminus (Cys-10 and Cys-12) that upon oxidation forms a disulfide bond. Disulfide formation rearranges a network of hydrogen bonds, which leads to a large conformational change of the protein and dissociation from DNA. MosR has been shown previously to play an important role in survival of the bacterium in the macrophage. In this study, we show that the main role of MosR is to up-regulate expression of rv1050 (a putative exported oxidoreductase that has not yet been characterized) in response to oxidants and propose that it is through this role that MosR contributes to the bacterium survival in the macrophage.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceBacterial ProteinsBase SequenceCrystallography, X-RayCysteineDisulfidesDNAElectrophoresis, Polyacrylamide GelGene Expression ProfilingHydrogen PeroxideModels, MolecularMolecular Sequence DataMutationMycobacterium tuberculosisNucleic Acid ConformationBacterial ProteinsCysteineDisulfidesDNAHydrogen PeroxideOxidantsTranscription Factors

Identifiers

PMID22992749
PMCPMC3488046
OpenAlexW2094577494

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.