Evidence map›Paper›PMID 16407278›Full record

ArticleThe Journal of biological chemistry2006

Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB.

Lee R Swem, Xing Gong, Chang-An Yu, Carl E Bauer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 92 citations in OpenAlex.

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  11. The SrrAB two-component system regulatesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Induction of theFrontiers in microbiology · 2020
    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

4 authors at 2 institutions in 1 country.

Lee R SwemDepartment of Biology, Indiana University, Bloomington, Indiana 47405, USA.
Xing Gong
Chang-An Yu
Carl E Bauer
Indiana University Bloomington · USOklahoma State University · US

Funding

Prokaryotic gene regulation by light and oxygenR37GM040941 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BAUER, CARL EUGENE · 2006 to 2016
$5.4M
REACTION MECHANISM OF MYOCARDIAC UBIQUINONE-PROTEINSR37GM030721 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI YU, CHANG-AN · 2000 to 2009
$4.6M
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
REACTION MECHANISMS OF MYOCARDIAL UBIQUINONE-PROTEINSR01GM030721 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI YU, CHANG-AN · 1985 to 1999
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NIGMS NIH HHS GM30721NIGMS NIH HHS GM53940NIGMS NIH HHS R01 GM030721NIGMS NIH HHS R01 GM040941NIGMS NIH HHS R01 GM053940NIGMS NIH HHS R37 GM030721NIGMS NIH HHS R37 GM040941
6 · The paper itself

Abstract

Rhodobacter capsulatus regulates many metabolic processes in response to the level of environmental oxygen and the energy state of the cell. One of the key global redox regulators of the cell's metabolic physiology is the sensor kinase RegB that controls the synthesis of numerous energy generation and utilization processes. In this study, we have succeeded in purifying full-length RegB containing six transmembrane-spanning elements. Exogenous addition of excess oxidized coenzyme Q1 is capable of inhibiting RegB autophosphorylation approximately 6-fold. However, the addition of reduced coenzyme Q1 exhibits no inhibitory effect on kinase activity. A ubiquinone-binding site, as defined by azidoquinone photo affinity cross-linking, was determined to lie within a periplasmic loop between transmembrane helices 3 and 4 that contains a fully conserved heptapeptide sequence of GGXXNPF. Mutation of the phenylalanine in this heptapeptide renders RegB constitutively active in vivo, indicating that this domain is responsible for sensing the redox state of the ubiquinone pool and subsequently controlling RegB autophosphorylation.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesBlotting, NorthernDNA Mutational AnalysisMolecular Sequence DataOxidation-ReductionPhosphorylationProtein KinasesProtein Structure, SecondaryProtein Structure, TertiaryRhodobacter capsulatusSpectrophotometryUbiquinoneBacterial ProteinsProtein KinasesRegB protein, RhodobacterUbiquinone

Identifiers

PMID16407278
PMCPMC2776112
OpenAlexW2035115681

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.