Evidence map›Paper›PMID 12970182›Full record

ArticleThe EMBO journal2003

Signal transduction by the global regulator RegB is mediated by a redox-active cysteine.

Lee R Swem, Brian J Kraft, Danielle L Swem, Aaron T Setterdahl, Shinji Masuda, David B Knaff, Jeffrey M Zaleski, Carl E Bauer

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
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  6. Article
  7. Article
  8. Article
  9. The SrrAB two-component system regulatesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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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

8 authors at 1 institution in 1 country.

Lee R SwemDepartment of Biology, Indiana University, Bloomington, IN 47405, USA.
Brian J Kraft
Danielle L Swem
Aaron T Setterdahl
Shinji Masuda
David B Knaff
Jeffrey M Zaleski
Carl E Bauer
Indiana University Bloomington · US

Funding

Prokaryotic gene regulation by light and oxygenR37GM040941 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BAUER, CARL EUGENE · 2006 to 2016
$5.4M
PROKARYOTIC GENE REGULATION BY LIGHT AND OXYGENR01GM040941 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BAUER, CARL EUGENE · 1994 to 2020
$3.3M
GENETIC ANALYSIS OF MG-TETRAPYRROLE BIOSYNTHESISR01GM053940 · NIGMS · INDIANA UNIVERSITY BLOOMINGTON · PI BAUER, CARL EUGENE · 1996 to 2005
$1.0M
NIGMS NIH HHS GM53940NIGMS NIH HHS R01 GM040941NIGMS NIH HHS R01 GM053940NIGMS NIH HHS R37 GM040941
6 · The paper itself

Abstract

All living organisms alter their physiology in response to changes in oxygen tension. The photosynthetic bacterium uses the RegB-RegA signal transduction cascade to control a wide variety of oxygen-responding processes such as respiration, photosynthesis, carbon fixation and nitrogen fixation. We demonstrate that a highly conserved cysteine has a role in controlling the activity of the sensor kinase, RegB. In vitro studies indicate that exposure of RegB to oxidizing conditions results in the formation of an intermolecular disulfide bond and that disulfide bond formation is metal-dependent, with the metal fulfilling a structural role. Formation of a disulfide bond in vitro is also shown to convert the kinase from an active dimer into an inactive tetramer state. Mutational analysis indicates that a cysteine residue flanked by cationic amino acids is involved in redox sensing in vitro and in vivo. These residues appear to constitute a novel 'redox-box' that is present in sensor kinases from diverse species of bacteria.

Indexed as

Bacterial ProteinsCysteineProtein KinasesAmino Acid SequenceMolecular Sequence DataOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsRhodobacter capsulatusSequence AlignmentSequence Homology, Amino AcidSignal TransductionBacterial ProteinsCysteinePhotosynthetic Reaction Center Complex ProteinsProtein KinasesRegB protein, Rhodobacter

Identifiers

PMID12970182
PMCPMC212728
OpenAlexW2060104088

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.