Evidence map›Paper›PMID 31465450›Full record

ArticlePLoS genetics2019

The (p)ppGpp-binding GTPase Era promotes rRNA processing and cold adaptation in Staphylococcus aureus.

Alison Wood, Sophie E Irving, Daniel J Bennison, Rebecca M Corrigan

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Nanoluciferase-Based Reporters for Clostridioides difficile.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Review
  5. DNA aptamer AptScientific reports · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. ClinicalmSphere · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. (p)ppGpp and Its Role in Bacterial Persistence: New Challenges.Antimicrobial agents and chemotherapy · 2020
    Review
  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

4 authors at 1 institution in 1 country.

Alison WoodThe Florey Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.ORCID 0000-0002-3366-727X
Sophie E IrvingThe Florey Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.ORCID 0000-0003-0772-1946
Daniel J BennisonThe Florey Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.
Rebecca M CorriganThe Florey Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.ORCID 0000-0002-6031-1148
University of Sheffield · GB

Funding

Medical Research CouncilWellcome TrustWellcome Trust 104110/Z/14/Z
6 · The paper itself

Abstract

Ribosome assembly cofactors are widely conserved across all domains of life. One such group, the ribosome-associated GTPases (RA-GTPase), act as molecular switches to coordinate ribosome assembly. We previously identified the Staphylococcus aureus RA-GTPase Era as a target for the stringent response alarmone (p)ppGpp, with binding leading to inhibition of GTPase activity. Era is highly conserved throughout the bacterial kingdom and is essential in many species, although the function of Era in ribosome assembly is unclear. Here we show that Era is not essential in S. aureus but is important for 30S ribosomal subunit assembly. Protein interaction studies reveal that Era interacts with the 16S rRNA endonuclease YbeY and the DEAD-box RNA helicase CshA. We determine that both Era and CshA are required for growth at suboptimal temperatures and rRNA processing. Era and CshA also form direct interactions with the (p)ppGpp synthetase RelSau, with RelSau positively impacting the GTPase activity of Era but negatively affecting the helicase activity of CshA. We propose that in its GTP-bound form, Era acts as a hub protein on the ribosome to direct enzymes involved in rRNA processing/degradation and ribosome subunit assembly to their site of action. This activity is impeded by multiple components of the stringent response, contributing to the slowed growth phenotype synonymous with this stress response pathway.

Indexed as

AcclimatizationBacterial ProteinsCold TemperatureDEAD-box RNA HelicasesEndonucleasesGTP-Binding ProteinsLigasesOrganelle BiogenesisProtein BindingProtein Interaction MappingRibosome Subunits, Small, BacterialRNA, RibosomalStaphylococcus aureusBacterial ProteinsDEAD-box RNA HelicasesEndonucleasesGTP-Binding Proteinsguanosine 3',5'-polyphosphate synthetasesLigasesRNA, Ribosomal

Identifiers

PMID31465450
PMCPMC6738653
OpenAlexW2971098387

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.