Evidence map›Paper›PMID 27628932›Full record

ArticleScientific reports2016

Fine-tuning of amino sugar homeostasis by EIIA(Ntr) in Salmonella Typhimurium.

Woongjae Yoo, Hyunjin Yoon, Yeong-Jae Seok, Chang-Ro Lee, Hyung Ho Lee, Sangryeol Ryu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. A Nitrogen Metabolic Enzyme ProvidesACS infectious diseases · 2021
    Article
  6. Review
  7. Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Enzyme IIAScientific reports · 2017
    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

6 authors at 3 institutions in 1 country.

Woongjae YooDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Korea.
Hyunjin YoonDepartment of Molecular Science and Technology, Department of Applied Chemistry and Biological Engineering, Ajou University, Suwon 16499, Korea.
Yeong-Jae SeokDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 08826, Korea.
Chang-Ro LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido 17058, Republic of Korea.
Hyung Ho LeeDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Korea.
Sangryeol RyuDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Research Institute for Agriculture and Life Sciences, and Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Korea.
Seoul National University · KRAjou University · KRMyongji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nitrogen-metabolic phosphotransferase system, PTS(Ntr), consists of the enzymes I(Ntr), NPr and IIA(Ntr) that are encoded by ptsP, ptsO, and ptsN, respectively. Due to the proximity of ptsO and ptsN to rpoN, the PTS(Ntr) system has been postulated to be closely related with nitrogen metabolism. To define the correlation between PTS(Ntr) and nitrogen metabolism, we performed ligand fishing with EIIA(Ntr) as a bait and revealed that D-glucosamine-6-phosphate synthase (GlmS) directly interacted with EIIA(Ntr). GlmS, which converts D-fructose-6-phosphate (Fru6P) into D-glucosamine-6-phosphate (GlcN6P), is a key enzyme producing amino sugars through glutamine hydrolysis. Amino sugar is an essential structural building block for bacterial peptidoglycan and LPS. We further verified that EIIA(Ntr) inhibited GlmS activity by direct interaction in a phosphorylation-state-dependent manner. EIIA(Ntr) was dephosphorylated in response to excessive nitrogen sources and was rapidly degraded by Lon protease upon amino sugar depletion. The regulation of GlmS activity by EIIA(Ntr) and the modulation of glmS translation by RapZ suggest that the genes comprising the rpoN operon play a key role in maintaining amino sugar homeostasis in response to nitrogen availability and the amino sugar concentration in the bacterial cytoplasm.

Indexed as

Amino SugarsBacterial ProteinsCytoplasmFructosephosphatesGlucosamineGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)HomeostasisNitrogenPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationSalmonella typhimuriumAmino SugarsBacterial Proteinscomponent S, glutamate mutase protein, Bacteriafructose-6-phosphateFructosephosphatesGlucosamineglucosamine 6-phosphateGlucose-6-PhosphateGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)NitrogenPhosphoenolpyruvate Sugar Phosphotransferase System

Identifiers

PMID27628932
PMCPMC5024086
OpenAlexW2519952988

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.