Evidence map›Paper›PMID 26574511›Full record

ArticleJournal of bacteriology2016

2-Aminoacrylate Stress Induces a Context-Dependent Glycine Requirement in ridA Strains of Salmonella enterica.

Dustin C Ernst, Diana M Downs

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2016. 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
3.0field-weighted citation impact, top 8% 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, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Advances in sRNA-mediated regulation ofFrontiers in cellular and infection microbiology · 2025
    Review
  4. Article
  5. Article
  6. RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Small RNA GcvB Regulates Oxidative Stress Response ofAntioxidants (Basel, Switzerland) · 2021
    Article
  13. RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Dustin C ErnstDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.
Diana M DownsDepartment of Microbiology, University of Georgia, Athens, Georgia, USA dmdowns@uga.edu.
University of Georgia · US

Funding

Rid family members neutralize endogenous metabolic stressorsR01GM095837 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DOWNS, DIANA M. · 2011 to 2023
$3.7M
NIGMS NIH HHS GM095837NIGMS NIH HHS R01 GM095837
6 · The paper itself

Abstract

unlabelledThe reactive enamine 2-aminoacrylate (2AA) is a metabolic stressor capable of damaging cellular components. Members of the broadly conserved Rid (RidA/YER057c/UK114) protein family mitigate 2AA stress in vivo by facilitating enamine and/or imine hydrolysis. Previous work showed that 2AA accumulation in ridA strains of Salmonella enterica led to the inactivation of multiple target enzymes, including serine hydroxymethyltransferase (GlyA). However, the specific cause of a ridA strain's inability to grow during periods of 2AA stress had yet to be determined. Work presented here shows that glycine supplementation suppressed all 2AA-dependent ridA strain growth defects described to date. Depending on the metabolic context, glycine appeared to suppress ridA strain growth defects by eliciting a GcvB small RNA-dependent regulatory response or by serving as a precursor to one-carbon units produced by the glycine cleavage complex (GCV). In either case, the data suggest that GlyA is the most physiologically sensitive target of 2AA inactivation in S. enterica. The universally conserved nature of GlyA among free-living organisms highlights the importance of RidA in mitigating 2AA stress. IMPORTANCE: The RidA stress response prevents 2-aminoacrylate (2AA) damage from occurring in prokaryotes and eukaryotes alike. 2AA inactivation of serine hydroxymethyltransferase (GlyA) from Salmonella enterica restricts glycine and one-carbon production, ultimately reducing fitness of the organism. The cooccurrence of genes encoding 2AA production enzymes and serine hydroxy-methyltransferase (SHMT) in many genomes may in part underlie the evolutionary selection for Rid proteins to maintain appropriate glycine and one-carbon metabolism throughout life.

Indexed as

AcrylatesBacterial ProteinsGene Expression Regulation, BacterialGlycineSalmonella entericaStress, PhysiologicalAcrylatesBacterial ProteinsGlycine

Identifiers

PMID26574511
PMCPMC4719459
OpenAlexW2204620269

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.