ArticleeLife2014
Prion propagation can occur in a prokaryote and requires the ClpB chaperone.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Review
- Characterization of an amyloid-based antiphage defence system in Escherichia coli.Nature microbiology · 2025Article
- The Transformation Experiment of Frederick Griffith I: Its Narrowing and Potential for the Creation of Novel Microorganisms.Bioengineering (Basel, Switzerland) · 2025Review
- The emergence of bacterial prions.PLoS pathogens · 2024Review
- Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Measuring prion propagation in single bacteria elucidates mechanism of loss.bioRxiv : the preprint server for biology · 2023Article
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Article
- A bacteria-based genetic assay detects prion formation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins ofFrontiers in molecular biosciences · 2019Article
- Evolutionary behaviour of bacterial prion-like proteins.PloS one · 2019Article
- Microbial specialization by prions.Prion · 2018Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- Article
- A bacterial global regulator forms a prion.Science (New York, N.Y.) · 2017Article
- Prion-Like Domains in Phagobiota.Frontiers in microbiology · 2017Article
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Journal of molecular biology · 2016Review
- Mammalian prion amyloid formation in bacteria.Prion · 2016Article
- Identification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid Formation.Frontiers in microbiology · 2016Article
- Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.Microbial cell factories · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies. Prions have also been uncovered in fungi, where they act as heritable, protein-based genetic elements. We previously showed that the yeast prion protein Sup35 can access the prion conformation in Escherichia coli. Here, we demonstrate that E. coli can propagate the Sup35 prion under conditions that do not permit its de novo formation. Furthermore, we show that propagation requires the disaggregase activity of the ClpB chaperone. Prion propagation in yeast requires Hsp104 (a ClpB ortholog), and prior studies have come to conflicting conclusions about ClpB's ability to participate in this process. Our demonstration of ClpB-dependent prion propagation in E. coli suggests that the cytoplasmic milieu in general and a molecular machine in particular are poised to support protein-based heredity in the bacterial domain of life.
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Registered trials
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.