Evidence map›Paper›PMID 32994436›Full record

ArticleScientific reports2020

Uridine diphosphate N-acetylglucosamine orchestrates the interaction of GlmR with either YvcJ or GlmS in Bacillus subtilis.

Elodie Foulquier, Frédérique Pompeo, Deborah Byrne, Henri-Pierre Fierobe, Anne Galinier

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Metabolic Redox Modulation byMolecules (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025
    Article
  6. Microbial Production ofFoods (Basel, Switzerland) · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Adaptation ofMicroorganisms · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Mutations inmBio · 2023
    Article
  17. Review
  18. Article
  19. Article
  20. The Natural AntimicrobialFoods (Basel, Switzerland) · 2021
    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 4 institutions in 1 country.

Elodie FoulquierLaboratoire de Chimie Bactérienne, UMR7283, Institut de Microbiologie de La Méditerranée, CNRS, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France.
Frédérique PompeoLaboratoire de Chimie Bactérienne, UMR7283, Institut de Microbiologie de La Méditerranée, CNRS, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France.
Deborah ByrneInstitut de Microbiologie de La Méditerranée, Protein Expression Facility, CNRS, Aix Marseille Université, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France.
Henri-Pierre FierobeLaboratoire de Chimie Bactérienne, UMR7283, Institut de Microbiologie de La Méditerranée, CNRS, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France.
Anne GalinierLaboratoire de Chimie Bactérienne, UMR7283, Institut de Microbiologie de La Méditerranée, CNRS, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France. galinier@imm.cnrs.fr.
Laboratoire de Chimie Bactérienne · FRAix-Marseille Université · FRCentre National de la Recherche Scientifique · FRInstitut de Microbiologie de la Méditerranée · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria, glucosamine-6-phosphate (GlcN6P) synthase, GlmS, is an enzyme required for the synthesis of Uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a precursor of peptidoglycan. In Bacillus subtilis, an UDP-GlcNAc binding protein, GlmR (formerly YvcK), essential for growth on non-glycolytic carbon sources, has been proposed to stimulate GlmS activity; this activation could be antagonized by UDP-GlcNAc. Using purified proteins, we demonstrate that GlmR directly stimulates GlmS activity and the presence of UDP-GlcNAc (at concentrations above 0.1 mM) prevents this regulation. We also showed that YvcJ, whose gene is associated with yvcK (glmR), interacts with GlmR in an UDP-GlcNAc dependent manner. Strains producing GlmR variants unable to interact with YvcJ show decreased transformation efficiency similar to that of a yvcJ null mutant. We therefore propose that, depending on the intracellular concentration of UDP-GlcNAc, GlmR interacts with either YvcJ or GlmS. When UDP-GlcNAc concentration is high, this UDP-sugar binds to YvcJ and to GlmR, blocking the stimulation of GlmS activity and driving the interaction between GlmR and YvcJ to probably regulate the cellular role of the latter. When the UDP-GlcNAc level is low, GlmR does not interact with YvcJ and thus does not regulate its cellular role but interacts with GlmS to stimulate its activity.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsCell WallGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)PeptidoglycanUridine DiphosphateUridine Diphosphate N-AcetylglucosamineBacterial Proteinscomponent S, glutamate mutase protein, BacteriaGlutamine-Fructose-6-Phosphate Transaminase (Isomerizing)PeptidoglycanUridine DiphosphateUridine Diphosphate N-Acetylglucosamine

Identifiers

PMID32994436
PMCPMC7525490
OpenAlexW3091212623

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.