Evidence map›Paper›PMID 26635369›Full record

ArticleThe Journal of biological chemistry2016

The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis.

Ksenia Hauf, Airat Kayumov, Felix Gloge, Karl Forchhammer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. The Functionality of IbpA fromInternational journal of molecular sciences · 2023
    Article
  4. Review
  5. Alanine synthesized by alanine dehydrogenase enables ammonium-tolerant nitrogen fixation inProceedings of the National Academy of Sciences of the United States of America · 2022
    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 2 countries.

Ksenia HaufFrom the Interfaculty Institute for Microbiology and Infection Medicine, University of Tuebingen, Auf der Morgenstelle 28, 72076 Tuebingen, Germany.
Airat Kayumovthe Department of Genetics, Kazan Federal University, Kremlevskaya 18, 420008, Kazan, Russia, and.
Felix GlogeWyatt Technology Europe, Hochstrasse 12a, 56307 Dernbach, Germany.
Karl ForchhammerFrom the Interfaculty Institute for Microbiology and Infection Medicine, University of Tuebingen, Auf der Morgenstelle 28, 72076 Tuebingen, Germany, karl.forchhammer@uni-tuebingen.de.
University of Tübingen · DEKazan Federal University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TnrA is a master regulator of nitrogen assimilation in Bacillus subtilis. This study focuses on the mechanism of how glutamine synthetase (GS) inhibits TnrA function in response to key metabolites ATP, AMP, glutamine, and glutamate. We suggest a model of two mutually exclusive GS conformations governing the interaction with TnrA. In the ATP-bound state (A-state), GS is catalytically active but unable to interact with TnrA. This conformation was stabilized by phosphorylated L-methionine sulfoximine (MSX), fixing the enzyme in the transition state. When occupied by glutamine (or its analogue MSX), GS resides in a conformation that has high affinity for TnrA (Q-state). The A- and Q-state are mutually exclusive, and in agreement, ATP and glutamine bind to GS in a competitive manner. At elevated concentrations of glutamine, ATP is no longer able to bind GS and to bring it into the A-state. AMP efficiently competes with ATP and prevents formation of the A-state, thereby favoring GS-TnrA interaction. Surface plasmon resonance analysis shows that TnrA bound to a positively regulated promoter fragment binds GS in the Q-state, whereas it rapidly dissociates from a negatively regulated promoter fragment. These data imply that GS controls TnrA activity at positively controlled promoters by shielding the transcription factor in the DNA-bound state. According to size exclusion and multiangle light scattering analysis, the dodecameric GS can bind three TnrA dimers. The highly interdependent ligand binding properties of GS reveal this enzyme as a sophisticated sensor of the nitrogen and energy state of the cell to control the activity of DNA-bound TnrA.

Indexed as

Models, MolecularPromoter Regions, GeneticAdenosine MonophosphateAdenosine TriphosphateBacillus subtilisBacterial ProteinsBinding, CompetitiveBinding SitesEnzyme StabilityGene DeletionGlutamate-Ammonia LigaseGlutamic AcidGlutamineKineticsLigandsMethionine SulfoximineAdenosine MonophosphateAdenosine TriphosphateBacterial ProteinsGlutamate-Ammonia LigaseGlutamic AcidGlutamineLigandsMethionine Sulfoximinemethionine sulfoximine phosphateRecombinant ProteinsRepressor ProteinsScgR protein, Bacillus subtilisAMPATPBacillus subtilisglutamateglutamineglutamine synthetasetranscription factor TnrAtranscription regulation

Identifiers

PMID26635369
PMCPMC4751389
OpenAlexW2183867307

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.