Evidence map›Paper›PMID 27432510›Full record

ArticleNature communications2016

The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core.

Karthik V Rajasekar, Konrad Zdanowski, Jun Yan, Jonathan T S Hopper, Marie-Louise R Francis, Colin Seepersad, Connor Sharp, Ludovic Pecqueur, Jörn M Werner, Carol V Robinson and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Conformational exchange at a CStructure (London, England : 1993) · 2023
    Article
  4. Expanding the genetic toolkit helps dissect a global stress response in the early-branching speciesProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Mechanisms of Action of Non-Canonical ECF Sigma Factors.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
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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

13 authors at 3 institutions in 1 country.

Karthik V RajasekarDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Konrad ZdanowskiDepartment of Biology, University of York, York YO10 5DD, UK.
Jun YanChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Jonathan T S HopperChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Marie-Louise R FrancisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Colin SeepersadDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Connor SharpDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Ludovic PecqueurSchool of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK.
Jörn M WernerSchool of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK.
Carol V RobinsonChemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford OX1 3TA, UK.
Shabaz MohammedDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.ORCID 0000-0003-2640-9560
Jennifer R PottsDepartment of Biology, University of York, York YO10 5DD, UK.
Colin KleanthousDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
University of Oxford · GBUniversity of Southampton · GBUniversity of York · GB

Funding

British Heart Foundation FS/12/36/29588Wellcome Trust
6 · The paper itself

Abstract

Redox-regulated effector systems that counteract oxidative stress are essential for all forms of life. Here we uncover a new paradigm for sensing oxidative stress centred on the hydrophobic core of a sensor protein. RsrA is an archetypal zinc-binding anti-sigma factor that responds to disulfide stress in the cytoplasm of Actinobacteria. We show that RsrA utilizes its hydrophobic core to bind the sigma factor σ(R) preventing its association with RNA polymerase, and that zinc plays a central role in maintaining this high-affinity complex. Oxidation of RsrA is limited by the rate of zinc release, which weakens the RsrA-σ(R) complex by accelerating its dissociation. The subsequent trigger disulfide, formed between specific combinations of RsrA's three zinc-binding cysteines, precipitates structural collapse to a compact state where all σ(R)-binding residues are sequestered back into its hydrophobic core, releasing σ(R) to activate transcription of anti-oxidant genes.

Indexed as

Hydrophobic and Hydrophilic InteractionsOxidative StressAmino Acid SequenceBacterial ProteinsCysteineKineticsMagnetic Resonance SpectroscopyOxidation-ReductionSigma FactorZincBacterial ProteinsCysteineSigma FactorZinc

Identifiers

PMID27432510
PMCPMC4960319
OpenAlexW2466491388

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.