Evidence map›Paper›PMID 30496454›Full record

ArticleNucleic acids research2019

Regulation of (p)ppGpp hydrolysis by a conserved archetypal regulatory domain.

Séverin Ronneau, Julien Caballero-Montes, Jérôme Coppine, Aurélie Mayard, Abel Garcia-Pino, Régis Hallez

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
11.2field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. Coupling of cell growth modulation to asymmetric division and cell cycle regulation inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. At the Crossroad of Nucleotide Dynamics and Protein Synthesis in Bacteria.Microbiology and molecular biology reviews : MMBR · 2023
    Review
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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

6 authors at 2 institutions in 1 country.

Séverin RonneauBacterial Cell cycle & Development (BCcD), Biology of Microorganisms Research Unit (URBM), Namur Research Institute for Life Science (NARILIS), University of Namur, 61 Rue de Bruxelles, 5000 Namur, Belgium.
Julien Caballero-MontesCellular and Molecular Microbiology, Université Libre de Bruxelles (ULB), 12 Rue des Professeurs Jeener et Brachet, B-6041 Gosselies, Belgium.
Jérôme CoppineBacterial Cell cycle & Development (BCcD), Biology of Microorganisms Research Unit (URBM), Namur Research Institute for Life Science (NARILIS), University of Namur, 61 Rue de Bruxelles, 5000 Namur, Belgium.
Aurélie MayardBacterial Cell cycle & Development (BCcD), Biology of Microorganisms Research Unit (URBM), Namur Research Institute for Life Science (NARILIS), University of Namur, 61 Rue de Bruxelles, 5000 Namur, Belgium.
Abel Garcia-PinoCellular and Molecular Microbiology, Université Libre de Bruxelles (ULB), 12 Rue des Professeurs Jeener et Brachet, B-6041 Gosselies, Belgium.
Régis HallezBacterial Cell cycle & Development (BCcD), Biology of Microorganisms Research Unit (URBM), Namur Research Institute for Life Science (NARILIS), University of Namur, 61 Rue de Bruxelles, 5000 Namur, Belgium.
University of Namur · BEUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sensory and regulatory domains allow bacteria to adequately respond to environmental changes. The regulatory ACT (Aspartokinase, Chorismate mutase and TyrA) domains are mainly found in metabolic-related proteins as well as in long (p)ppGpp synthetase/hydrolase enzymes. Here, we investigate the functional role of the ACT domain of SpoT, the only (p)ppGpp synthetase/hydrolase of Caulobacter crescentus. We show that SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. In addition, our in vivo and in vitro data show that the phosphorylated version of EIIANtr (EIIANtr∼P) interacts directly with the ACT and inhibits the hydrolase activity of SpoT. Finally, we highlight the conservation of the ACT-dependent interaction between EIIANtr∼P and SpoT/Rel along with the phosphotransferase system (PTSNtr)-dependent regulation of (p)ppGpp accumulation upon nitrogen starvation in Sinorhizobium meliloti, a plant-associated α-proteobacterium. Thus, this work suggests that α-proteobacteria might have inherited from a common ancestor, a PTSNtr dedicated to modulate (p)ppGpp levels in response to nitrogen availability.

Indexed as

Bacterial ProteinsCaulobacter crescentusGuanosine PentaphosphateHydrolasesHydrolysisLigasesProtein DomainsProtein Interaction Domains and MotifsSinorhizobium melilotiBacterial Proteinsguanosine 3',5'-polyphosphate synthetasesGuanosine PentaphosphateHydrolasesLigases

Identifiers

PMID30496454
PMCPMC6344854
OpenAlexW2949607783

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.