Evidence map›Paper›PMID 23306201›Full record

ArticleThe Journal of biological chemistry2013

RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid.

Jiang Wu, Zhuo Cheng, Khalilah Reddie, Kate Carroll, Loubna A Hammad, Jonathan A Karty, Carl E Bauer

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Persulfidation of Human CystathionineAntioxidants (Basel, Switzerland) · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. HAntioxidants (Basel, Switzerland) · 2021
    Article
  8. Endogenous SORedox biology · 2021
    Article
  9. Article
  10. Article
  11. The SrrAB two-component system regulatesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

7 authors.

Jiang WuDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
Zhuo Cheng
Khalilah Reddie
Kate Carroll
Loubna A Hammad
Jonathan A Karty
Carl E Bauer

Funding

Prokaryotic gene regulation by light and oxygenR37GM040941 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BAUER, CARL EUGENE · 2006 to 2016
$5.4M
Probing the role of cysteine sulfenylation in cell signalingR01GM102187 · NIGMS · UNIVERSITY OF FLORIDA · PI Kate Suzanne Carroll · 2012 to 2026
$4.6M
PROKARYOTIC GENE REGULATION BY LIGHT AND OXYGENR01GM040941 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BAUER, CARL EUGENE · 1994 to 2020
$3.3M
Nucleophilic Inhibitors for Targeting Redox-Sensitive KinasesR01CA174864 · NCI · SCRIPPS FLORIDA · PI CARROLL, KATE SUZANNE · 2014 to 2017
$1.6M
NCI NIH HHS R01 CA174864NIGMS NIH HHS R01 GM040941NIGMS NIH HHS R01 GM102187NIGMS NIH HHS R37 GM040941
6 · The paper itself

Abstract

RegB/RegA comprise a global redox-sensing signal transduction system utilized by a wide range of proteobacteria to sense environmental changes in oxygen tension. The conserved cysteine 265 in the sensor kinase RegB was previously reported to form an intermolecular disulfide bond under oxidizing conditions that converts RegB from an active dimer into an inactive tetramer. In this study, we demonstrate that a stable sulfenic acid (-SOH) derivative also forms at Cys-265 in vitro and in vivo when RegB is exposed to oxygen. This sulfenic acid modification is reversible and stable in the air. Autophosphorylation assay shows that reduction of the SOH at Cys-265 to a free thiol (SH) can increase RegB kinase activity in vitro. Our results suggest that a sulfenic acid modification at Cys-265 performs a regulatory role in vivo and that it may be the major oxidation state of Cys-265 under aerobic conditions. Cys-265 thus functions as a complex redox switch that can form multiple thiol modifications in response to different redox signals to control the kinase activity of RegB.

Indexed as

Gene Expression Regulation, EnzymologicBacterial ProteinsBiotinylationCysteineHistidine KinaseMass SpectrometryModels, BiologicalOxidation-ReductionOxygenPhosphorylationProtein BindingProtein KinasesRhodobacter capsulatusSignal TransductionSulfenic AcidsSulfhydryl CompoundsBacterial ProteinsCysteineHistidine KinaseOxygenProtein KinasesRegB protein, RhodobacterSulfenic AcidsSulfhydryl CompoundsUbiquinone

Identifiers

PMID23306201
PMCPMC3576080

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.