Evidence map›Paper›PMID 23354745›Full record

ArticleJournal of bacteriology2013

Two roles for aconitase in the regulation of tricarboxylic acid branch gene expression in Bacillus subtilis.

Kieran B Pechter, Frederik M Meyer, Alisa W Serio, Jörg Stülke, Abraham L Sonenshein

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Moonlighting inMicroorganisms · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Intermolecular Communication inFrontiers in molecular biosciences · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Secreted Citrate Serves as Iron Carrier for the Marine PathogenFrontiers in cellular and infection microbiology · 2017
    Article
  17. Article
  18. 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

5 authors at 2 institutions in 2 countries.

Kieran B PechterProgram in Molecular Microbiology, Sackler School of Graduate Biomedical Sciences, Tufts University, Boston, MA, USA.
Frederik M Meyer
Alisa W Serio
Jörg Stülke
Abraham L Sonenshein
Tufts University · USUniversity of Göttingen · DE

Funding

REGULATION OF NITROGEN METABOLISM IN BACILLUS SUBTILISR01GM036718 · NIGMS · TUFTS UNIVERSITY BOSTON · PI BELITSKY, BORIS R, SONENSHEIN, ABRAHAM LINCOLN · 1986 to 2011
$3.2M
NIGMS NIH HHS R01 GM036718NIGMS NIH HHS R01GM036718
6 · The paper itself

Abstract

Previously, it was shown that an aconitase (citB) null mutation results in a vast overaccumulation of citrate in the culture fluid of growing Bacillus subtilis cells, a phenotype that causes secondary effects, including the hyperexpression of the citB promoter. B. subtilis aconitase is a bifunctional protein; to determine if either or both activities of aconitase were responsible for this phenotype, two strains producing different mutant forms of aconitase were constructed, one designed to be enzymatically inactive (C450S [citB2]) and the other designed to be defective in RNA binding (R741E [citB7]). The citB2 mutant was a glutamate auxotroph and accumulated citrate, while the citB7 mutant was a glutamate prototroph. Unexpectedly, the citB7 strain also accumulated citrate. Both mutant strains exhibited overexpression of the citB promoter and accumulated high levels of aconitase protein. These strains and the citB null mutant also exhibited increased levels of citrate synthase protein and enzyme activity in cell extracts, and the major citrate synthase (citZ) transcript was present at higher-than-normal levels in the citB null mutant, due at least in part to a >3-fold increase in the stability of the citZ transcript compared to the wild type. Purified B. subtilis aconitase bound to the citZ 5' leader RNA in vitro, but the mutant proteins did not. Together, these data suggest that wild-type aconitase binds to and destabilizes the citZ transcript in order to maintain proper cell homeostasis by preventing the overaccumulation of citrate.

Indexed as

Gene Expression Regulation, BacterialAconitate HydrataseBacillus subtilisBinding SitesCitric AcidCitric Acid CycleDNA, BacterialGene Expression ProfilingGlutamic AcidMutant ProteinsPromoter Regions, GeneticProtein BindingRNA-Binding ProteinsAconitate HydrataseCitric AcidDNA, BacterialGlutamic AcidMutant ProteinsRNA-Binding Proteins

Identifiers

PMID23354745
PMCPMC3624536
OpenAlexW1972417073

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.