ArticleFrontiers in microbiology2015
The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.
Article in Frontiers in microbiology, 2015. 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, 44 citations in OpenAlex.
- An intrinsically disordered domain of transcription terminator Rho governs genome-wide Rho utilization (Rut) site selection in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Distinct Spatial Organisation of Rho and RNA Polymerase in Salmonella Cells.Molecular microbiology · 2026Article
- The role of microbiota dysbiosis in Parkinson's disease: Pathophysiology and therapeutic opportunities.Engineering microbiology · 2025Review
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- Diversification of the Rho transcription termination factor in bacteria.Nucleic acids research · 2024Article
- The emergence of bacterial prions.PLoS pathogens · 2024Review
- Phase Variation of Flagella and Toxins in Clostridioides difficile is Mediated by Selective Rho-dependent Termination.Journal of molecular biology · 2024Article
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis.Life (Basel, Switzerland) · 2021Article
- Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions.International journal of molecular sciences · 2020Review
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids.mSystems · 2020Review
- AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity.BMC bioinformatics · 2019Article
- Article
- Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils.Scientific reports · 2018Article
- Transcription termination factor Rho and microbial phenotypic heterogeneity.Current genetics · 2018Review
- The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.International journal of molecular sciences · 2018Article
- Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans.Cell cycle (Georgetown, Tex.) · 2018Review
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion-like proteins can switch between a soluble intrinsically disordered conformation and a highly ordered amyloid assembly. This conformational promiscuity is encoded in specific sequence regions, known as prion domains (PrDs). Prions are best known as the causative factors of neurological diseases in mammals. However, bioinformatics analyses reveal that proteins bearing PrDs are present in all kingdoms of life, including bacteria, thus supporting the idea that they serve conserved beneficial cellular functions. Despite the proportion of predicted prion-like proteins in bacterial proteomes is generally low, pathogenic species seem to have a higher prionic load, suggesting that these malleable proteins may favor pathogenic traits. In the present work, we performed a stringent computational analysis of the Clostridium botulinum pathogen proteome in the search for prion-like proteins. A total of 54 candidates were predicted for this anaerobic bacterium, including the transcription termination Rho factor. This RNA-binding protein has been shown to play a crucial role in bacterial adaptation to changing environments. We show here that the predicted disordered PrD domain of this RNA-binding protein contains an inner, highly polar, asparagine-rich short sequence able to spontaneously self-assemble into amyloid-like structures, bearing thus the potential to induce a Rho factor conformational switch that might rewire gene expression in response to environmental conditions.
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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.