Evidence map›Paper›PMID 30366986›Full record

ArticleThe Journal of biological chemistry2018

Structural basis for (p)ppGpp-mediated inhibition of the GTPase RbgA.

Patrick Pausch, Wieland Steinchen, Maximiliane Wieland, Thomas Klaus, Sven-Andreas Freibert, Florian Altegoer, Daniel N Wilson, Gert Bange

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Suppressor analysis inFrontiers in microbiology · 2026
    Article
  4. Article
  5. ClinicalmSphere · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

8 authors at 2 institutions in 1 country.

Patrick PauschFrom the Department of Chemistry and Patrick.Pausch@synmikro.uni-marburg.de.
Wieland SteinchenFrom the Department of Chemistry and.
Maximiliane Wielandthe Institute for Biochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.
Thomas KlausFrom the Department of Chemistry and.
Sven-Andreas Freibertthe Synmikro Center for Synthetic Microbiology, 35043 Marburg, Germany, and.
Florian AltegoerFrom the Department of Chemistry and.
Daniel N Wilsonthe Institute for Biochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.
Gert BangeFrom the Department of Chemistry and Gert.Bange@synmikro.uni-marburg.de.
Loewe Center for Synthetic Microbiology · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient adaptation to environmental changes is pivotal for all bacterial cells. Almost all bacterial species depend on the conserved stringent response system to prompt timely transcriptional and metabolic responses according to stress conditions and nutrient depletion. The stringent response relies on the stress-dependent synthesis of the second messenger nucleotides and alarmones (p)ppGpp, which pleiotropically target and reprogram processes that consume cellular resources, such as ribosome biogenesis. Here we show that (p)ppGpp acts on the ribosome biogenesis GTPase A (RbgA) of Gram-positive bacteria. Using X-ray crystallography, hydrogen-deuterium exchange MS (HDX-MS) and kinetic analysis, we demonstrate that the alarmones (p)ppGpp bind to RbgA in a manner similar to that of binding by GDP and GTP and thereby act as competitive inhibitors. Our structural analysis of

Indexed as

Amino Acid SequenceBacillus subtilisCrystallography, X-RayEnzyme InhibitorsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine PentaphosphateGuanosine TriphosphateKineticsMagnesiumModels, MolecularProtein DomainsStaphylococcus aureusEnzyme InhibitorsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine PentaphosphateGuanosine TriphosphateMagnesiumalarmonecell stressenzyme kineticsGTPaseinhibition mechanism(p)ppGppRbgAribosome assemblystringent responseX-ray crystallography

Identifiers

PMID30366986
PMCPMC6314131
OpenAlexW2898103244

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.