Evidence map›Paper›PMID 17557830›Full record

ArticleJournal of bacteriology2007

Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1.

Yong-Jin Kim, In-Jeong Ko, Jin-Mok Lee, Ho-Young Kang, Young Min Kim, Samuel Kaplan, Jeong-Il Oh

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Regulation of bacterial photosynthesis genes by the small noncoding RNA PcrZ.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Nitrous oxide production and consumption: regulation of gene expression by gas-sensitive transcription factors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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.

Yong-Jin KimDepartment of Microbiology, Pusan National University, 30 Jangjeon-dong, Geumjeong-gu, 609-735 Busan, Korea.
In-Jeong Ko
Jin-Mok Lee
Ho-Young Kang
Young Min Kim
Samuel Kaplan
Jeong-Il Oh

Funding

INDUCTION AND BIOGENESIS OF SUBCELLULAR ORGANELLESR01GM015590 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI KAPLAN, SAMUEL · 1985 to 2008
$3.0M
NIGMS NIH HHS GM15590NIGMS NIH HHS R01 GM015590
6 · The paper itself

Abstract

In this study, the H303A mutant form of the cbb(3) oxidase (H303A oxidase), which has the H303A mutation in its catalytic subunit (CcoN), was purified from Rhodobacter sphaeroides. The H303A oxidase showed the same catalytic activity as did the wild-type form of the oxidase (WT oxidase). The heme contents of the mutant and WT forms of the cbb(3) oxidase were also comparable. However, the puf and puc operons, which are under the control of the PrrBA two-component system, were shown to be derepressed aerobically in the R. sphaeroides strain expressing the H303A oxidase. Since the strain harboring the H303A oxidase exhibited the same cytochrome c oxidase activity as the stain harboring the WT oxidase did, the aerobic derepression of photosynthesis gene expression observed in the H303A mutant appears to be the result of a defective signaling function of the H303A oxidase rather than reflecting any redox changes in the ubiquinone/ubiquinol pool. It was also demonstrated that ubiquinone inhibits not only the autokinase activity of full-length PrrB but also that of the truncated form of PrrB lacking its transmembrane domain, including the proposed quinone binding sequence. These results imply that the suggested ubiquinone binding site within the PrrB transmembrane domain is not necessary for the inhibition of PrrB kinase activity by ubiquinone. Instead, it is probable that signaling through H303 of the CcoN subunit of the cbb(3) oxidase is part of the pathway through which the cbb(3) oxidase affects the relative kinase/phosphatase activity of the membrane-bound PrrB.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SubstitutionBinding SitesElectron Transport Complex IVHistidine KinaseMutation, MissensePhosphorylationPhotosynthesisProtein KinasesRhodobacter sphaeroidesSignal TransductionUbiquinonecbb3 oxidaseElectron Transport Complex IVHistidine KinaseProtein KinasesUbiquinone

Identifiers

PMID17557830
PMCPMC1951837

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.