Evidence map›Paper›PMID 23517463›Full record

ArticleMolecular microbiology2013

Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and α-ketoglutarate in Escherichia coli.

Chang-Ro Lee, Young-Ha Park, Miri Kim, Yeon-Ran Kim, Soyoung Park, Alan Peterkofsky, Yeong-Jae Seok

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2013. 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
3.8field-weighted citation impact, top 6% 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, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. mSystems · 2026
    Article
  5. Article
  6. Article
  7. Regulation of phosphate starvation-specific responses inMicrobiology (Reading, England) · 2023
    Review
  8. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  9. Article
  10. Fosfomycin Resistance Evolutionary Pathways ofInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Global control of bacterial nitrogen and carbon metabolism by a PTSProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  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 at 3 institutions in 3 countries.

Chang-Ro LeeDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul, 151-742, Korea.
Young-Ha Park
Miri Kim
Yeon-Ran Kim
Soyoung Park
Alan Peterkofsky
Yeong-Jae Seok
New Generation University College · ETSeoul National University · KRNational Heart Lung and Blood Institute · US

Funding

Intramural NIH HHS Z99 HL999999
6 · The paper itself

Abstract

In addition to the phosphoenolpyruvate:sugar phosphotransferase system (sugar PTS), most proteobacteria possess a paralogous system (nitrogen phosphotransferase system, PTS(Ntr)). The first proteins in both pathways are enzymes (enzyme I(sugar) and enzyme I(Ntr)) that can be autophosphorylated by phosphoenolpyruvate. The most striking difference between enzyme I(sugar) and enzyme I(Ntr) is the presence of a GAF domain at the N-terminus of enzyme I(Ntr). Since the PTS(Ntr) was identified in 1995, it has been implicated in a variety of cellular processes in many proteobacteria and many of these regulations have been shown to be dependent on the phosphorylation state of PTS(Ntr) components. However, there has been little evidence that any component of this so-called PTS(Ntr) is directly involved in nitrogen metabolism. Moreover, a signal regulating the phosphorylation state of the PTS(Ntr) had not been uncovered. Here, we demonstrate that glutamine and α-ketoglutarate, the canonical signals of nitrogen availability, reciprocally regulate the phosphorylation state of the PTS(Ntr) by direct effects on enzyme I(Ntr) autophosphorylation and the GAF signal transduction domain is necessary for the regulation of enzyme I(Ntr) activity by the two signal molecules. Taken together, our results suggest that the PTS(Ntr) senses nitrogen availability.

Indexed as

Gene Expression Regulation, BacterialElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsGlutamineKetoglutaric AcidsNitrogenPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationPhosphotransferasesPlasmidsProtein EngineeringEscherichia coli ProteinsGlutamineKetoglutaric AcidsNitrogenPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphotransferasesPtsN protein, E coli

Identifiers

PMID23517463
PMCPMC3633653
OpenAlexW2146040892

What OpenQuestion holds

Textmetadata
LicenceTDM
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.