Evidence map›Paper›PMID 23479646›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR.

Quanjiang Ji, Liang Zhang, Marcus B Jones, Fei Sun, Xin Deng, Haihua Liang, Hoonsik Cho, Pedro Brugarolas, Yihe N Gao, Scott N Peterson and 3 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

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  9. Identification of Vitamin K3 and its analogues as covalent inhibitors of SARS-CoV-2 3CLInternational journal of biological macromolecules · 2021
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  10. Review
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  13. Molecular Mechanisms ofFrontiers in cellular and infection microbiology · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Two distinct mechanisms of transcriptional regulation by the redox sensor YodB.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

13 authors at 4 institutions in 2 countries.

Quanjiang JiDepartment of Chemistry, The University of Chicago, Chicago, IL 60637, USA.
Liang Zhang
Marcus B Jones
Fei Sun
Xin Deng
Haihua Liang
Hoonsik Cho
Pedro Brugarolas
Yihe N Gao
Scott N Peterson
Lefu Lan
Taeok Bae
Chuan He
University of Chicago · USIndiana University Northwest · USJ. Craig Venter Institute · USChinese Academy of Sciences · CN

Funding

CORE: ADMINISTRATIVEP50GM081892 · NIGMS · UNIVERSITY OF CHICAGO · PI WHITE, KEVIN P. · 2008 to 2013
$15.9M
Tuning Virulence Determinants in Staphylococcus aureusR01AI074658 · NIAID · UNIVERSITY OF CHICAGO · PI HE, CHUAN · 2007 to 2016
$3.8M
Prophage contribution to the virulence of Staphylococcus aureusR01AI077564 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI BAE, TAEOK · 2009 to 2013
$1.5M
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 AI074658NIAID NIH HHS R01 AI077564NIGMS NIH HHS P50 GM081892NIGMS NIH HHS P50GM081892
6 · The paper itself

Abstract

Quinone molecules are intracellular electron-transport carriers, as well as critical intra- and extracellular signals. However, transcriptional regulation of quinone signaling and its molecular basis are poorly understood. Here, we identify a thiol-stress-sensing regulator YodB family transcriptional regulator as a central component of quinone stress response of Staphylococcus aureus, which we have termed the quinone-sensing and response repressor (QsrR). We also identify and confirm an unprecedented quinone-sensing mechanism based on the S-quinonization of the essential residue Cys-5. Structural characterizations of the QsrR-DNA and QsrR-menadione complexes further reveal that the covalent association of menadione directly leads to the release of QsrR from operator DNA following a 10° rigid-body rotation as well as a 9-Å elongation between the dimeric subunits. The molecular level characterization of this quinone-sensing transcriptional regulator provides critical insights into quinone-mediated gene regulation in human pathogens.

Indexed as

Bacterial ProteinsBenzoquinonesRepressor ProteinsStaphylococcus aureusDNA, BacterialGene Expression Regulation, BacterialHumansProtein Processing, Post-TranslationalProtein Structure, QuaternaryProtein Structure, TertiarySignal TransductionBacterial ProteinsBenzoquinonesDNA, BacterialquinoneRepressor Proteins

Identifiers

PMID23479646
PMCPMC3612684
OpenAlexW1994944003

What OpenQuestion holds

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Registered trials

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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.