Evidence map›Paper›PMID 28082594›Full record

ArticleScience (New York, N.Y.)2017

A bacterial global regulator forms a prion.

Andy H Yuan, Ann Hochschild

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
10.1field-weighted citation impact, top 1% 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

100 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The prion-like characteristic of ORF3 contributes to virion release and pathogenesis of hepatitis E virus.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

40 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Andy H YuanDepartment of Microbiology and Immunobiology, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115, USA.
Ann HochschildDepartment of Microbiology and Immunobiology, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115, USA. ann_hochschild@hms.harvard.edu.
Harvard University · US

Funding

A new genetic approach for studying prions and other pathogenic protein aggregateDP1OD003806 · OD · HARVARD MEDICAL SCHOOL · PI HOCHSCHILD, ANN · 2008 to 2011
$3.4M
Amyloid aggregation and prion formation in bacteriaR01GM115941 · NIGMS · HARVARD MEDICAL SCHOOL · PI HOCHSCHILD, ANN · 2016 to 2019
$1.9M
NIGMS NIH HHS R01 GM115941NIH HHS DP1 OD003806
6 · The paper itself

Abstract

Prions are self-propagating protein aggregates that act as protein-based elements of inheritance in fungi. Although prevalent in eukaryotes, prions have not been identified in bacteria. Here we found that a bacterial protein, transcription terminator Rho of Clostridium botulinum (Cb-Rho), could form a prion. We identified a candidate prion-forming domain (cPrD) in Cb-Rho and showed that it conferred amyloidogenicity on Cb-Rho and could functionally replace the PrD of a yeast prion-forming protein. Furthermore, its cPrD enabled Cb-Rho to access alternative conformations in Escherichia coli-a soluble form that terminated transcription efficiently and an aggregated, self-propagating prion form that was functionally compromised. The prion form caused genome-wide changes in the transcriptome. Thus, Cb-Rho functions as a protein-based element of inheritance in bacteria, suggesting that the emergence of prions predates the evolutionary split between eukaryotes and bacteria.

Indexed as

Amino Acid SequenceAmyloidBacterial ProteinsClostridium botulinumEscherichia coliEvolution, MolecularPrionsProtein DomainsRho FactorSaccharomyces cerevisiae ProteinsAmyloidBacterial ProteinsPrionsRho FactorSaccharomyces cerevisiae Proteins

Identifiers

PMID28082594
PMCPMC5460984
OpenAlexW2577163397

What OpenQuestion holds

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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.