Evidence map›Paper›PMID 17803943›Full record

ArticleMolecular cell2007

A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria.

Elizabeth A Campbell, Roger Greenwell, Jennifer R Anthony, Sheng Wang, Lionel Lim, Kalyan Das, Heidi J Sofia, Timothy J Donohue, Seth A Darst

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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
  6. Article
  7. Mechanisms of Action of Non-Canonical ECF Sigma Factors.International journal of molecular sciences · 2022
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structural basis for transcription activation by Crl through tethering of σProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Zinc binding proteome of a phytopathogenRoyal Society open science · 2019
    Article
  19. Review
  20. Review

17 more citing papers are in PubMed but not listed here.

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 4 institutions in 1 country.

Elizabeth A CampbellThe Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Roger Greenwell
Jennifer R Anthony
Sheng Wang
Lionel Lim
Kalyan Das
Heidi J Sofia
Timothy J Donohue
Seth A Darst
University of Wisconsin–Madison · USRockefeller University · USPacific Northwest National Laboratory · USRutgers, The State University of New Jersey · US

Funding

E COLI RNA POLYMERASE SUBUNIT--STRUCTURE/FUNCTIONR01GM053759 · NIGMS · ROCKEFELLER UNIVERSITY · PI DARST, SETH A. · 1996 to 2015
$6.9M
Bacterial Response to Singlet OxygenR01GM075273 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DONOHUE, TIMOTHY J · 2006 to 2009
$1.1M
NIGMS NIH HHS GM053759NIGMS NIH HHS R01 GM053759NIGMS NIH HHS R01 GM075273
6 · The paper itself

Abstract

A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn(2+), and is required for the transcriptional response to singlet oxygen. Structure-based sequence analyses predict that the ASD defines a common structural fold among predicted group IV anti-sigmas. These ASDs are fused to diverse C-terminal domains that are likely involved in responding to specific environmental signals that control the activity of their cognate sigma factor.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayGene Expression Regulation, BacterialModels, MolecularMolecular Sequence DataOxygenProtein FoldingProtein Structure, TertiaryRhodobacter sphaeroidesSequence AlignmentSigma FactorTranscription FactorsTranscription, GeneticZincBacterial ProteinsChrR protein, Rhodobacter sphaeroidesOxygenrol protein, BacteriaSigma Factorsporulation-specific sigma factorsTranscription FactorsZinc

Identifiers

PMID17803943
PMCPMC2390684
OpenAlexW2155837642

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.