Evidence map›Paper›PMID 21157513›Full record

ArticlemBio2010

RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool.

Jiang Wu, Carl E Bauer

Open access · goldAbstract read
In one paragraph

Article in mBio, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The SrrAB two-component system regulatesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Review
  11. Induction of theFrontiers in microbiology · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Jiang WuDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
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
REGULATION OF PROCARYOTIC GENE EXPRESSION BY MOLECULARR29GM040941 · NIGMS · INDIANA UNIVERSITY BLOOMINGTON · PI BAUER, CARL EUGENE · 1989 to 1993
–
NIGMS NIH HHS GM40941NIGMS NIH HHS R01 GM040941NIGMS NIH HHS R37 GM040941
6 · The paper itself

Abstract

RegB is a membrane-spanning sensor kinase responsible for redox regulation of a wide variety of metabolic processes in numerous proteobacterial species. Here we show that full-length RegB purified from Escherichia coli membranes contains bound ubiquinone. Four conserved residues in the membrane-spanning domain of RegB are shown to have important roles in ubiquinone binding in vitro and redox sensing in vivo. Isothermal titration calorimetry measurements, coupled with kinase assays under oxidizing and reducing conditions, indicate that RegB weakly binds both oxidized ubiquinone and reduced ubiquinone (ubiquinol) with nearly equal affinity and that oxidized ubiquinone inhibits kinase activity without promoting a redox reaction. We propose a model in which ubiquinone/ubiquinol bound to RegB readily equilibrates with ubiquinones/ubiquinols in the membrane, allowing the kinase activity to be tuned by the redox state of the ubiquinone pool. This noncatalytic role of ubiquinone in controlling RegB activity is distinct from that of other known ubiquinone-binding proteins, which use ubiquinone as an electron donor or acceptor.

Indexed as

Amino Acid SequenceBacterial ProteinsEscherichia coliModels, BiologicalMolecular Sequence DataOxidation-ReductionProtein BindingProtein KinasesRecombinant ProteinsSequence AlignmentUbiquinoneBacterial ProteinsProtein KinasesRecombinant ProteinsRegB protein, RhodobacterubiquinolUbiquinone

Identifiers

PMID21157513
PMCPMC3000548
OpenAlexW2100535301

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.