Evidence map›Paper›PMID 32393900›Full record

ArticleNature chemical biology2020

A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes.

Hedvig Tamman, Katleen Van Nerom, Hiraku Takada, Niels Vandenberk, Daniel Scholl, Yury Polikanov, Johan Hofkens, Ariel Talavera, Vasili Hauryliuk, Jelle Hendrix and 1 more

Abstract read
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In one paragraph

Article in Nature chemical biology, 2020. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
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  5. The N-Terminal Extension of theAntibiotics (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Biochemical and X-ray analyses of the players involved in the faRel2/aTfaRel2 toxin-antitoxin operon.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  10. 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
  11. Identification of a broadly conserved family of enzymes that hydrolyze (p)ppApp.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. 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

11 authors.

Hedvig Tamman *Cellular and Molecular Microbiology, Faculté des Sciences, Université Libre de Bruxelles, Brussels, Belgium.
Katleen Van Nerom *Cellular and Molecular Microbiology, Faculté des Sciences, Université Libre de Bruxelles, Brussels, Belgium.
Hiraku TakadaDepartment of Molecular Biology, Umeå University, Umeå, Sweden.ORCID http://orcid.org/0000-0003-2034-5666
Niels VandenberkMolecular Imaging and Photonics, Chemistry Department, KU Leuven, Leuven, Belgium.
Daniel SchollSFMB, Université Libre de Bruxelles, Brussels, Belgium.
Yury PolikanovDepartment of Biological Sciences, College of Liberal Arts and Sciences, University of Illinois at Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-5064-0327
Johan HofkensMolecular Imaging and Photonics, Chemistry Department, KU Leuven, Leuven, Belgium.
Ariel TalaveraCMMI, Université Libre de Bruxelles, Gosselies, Belgium.ORCID http://orcid.org/0000-0002-1865-5959
Vasili HauryliukDepartment of Molecular Biology, Umeå University, Umeå, Sweden. vasili.hauryliuk@umu.se.ORCID http://orcid.org/0000-0003-2389-5057
Jelle HendrixMolecular Imaging and Photonics, Chemistry Department, KU Leuven, Leuven, Belgium. jelle.hendrix@uhasselt.be.ORCID http://orcid.org/0000-0001-5731-1297
Abel Garcia-PinoCellular and Molecular Microbiology, Faculté des Sciences, Université Libre de Bruxelles, Brussels, Belgium. agarciap@ulb.ac.be.ORCID http://orcid.org/0000-0002-0634-0300

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bifunctional Rel stringent factors, the most abundant class of RelA/SpoT homologs, are ribosome-associated enzymes that transfer a pyrophosphate from ATP onto the 3' of guanosine tri-/diphosphate (GTP/GDP) to synthesize the bacterial alarmone (p)ppGpp, and also catalyze the 3' pyrophosphate hydrolysis to degrade it. The regulation of the opposing activities of Rel enzymes is a complex allosteric mechanism that remains an active research topic despite decades of research. We show that a guanine-nucleotide-switch mechanism controls catalysis by Thermus thermophilus Rel (Rel

Indexed as

Amino Acid SequenceBacteriaBacterial ProteinsCatalytic DomainGene Expression Regulation, BacterialGenes, relGuanosine PentaphosphateGuanosine TetraphosphateHydrolasesLigasesNucleotidesProto-Oncogene Proteins c-relRibosomesThermus thermophilusBacterial Proteinsguanosine 3',5'-polyphosphate synthetasesGuanosine PentaphosphateGuanosine TetraphosphateHydrolasesLigasesNucleotidesProto-Oncogene Proteins c-rel

Identifiers

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.