ArticleScientific reports2016
Functional amyloids as inhibitors of plasmid DNA replication.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- Non-Vesicular Extracellular Particle (NVEP) Proteomes from Diverse Biological Sources Reveal Specific Marker Composition with Varying Enrichment Levels.Biomolecules · 2025Article
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- Dynamic transitions of initiator binding coordinate the replication of the two chromosomes in Vibrio cholerae.Nature communications · 2025Article
- The emergence of bacterial prions.PLoS pathogens · 2024Review
- Cell cycle-coordinated maintenance of theEcoSal Plus · 2023Review
- Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023Review
- p53, A Victim of the Prion Fashion.Cancers · 2021Review
- Multifunctional Amyloids in the Biology of Gram-Positive Bacteria.Microorganisms · 2020Review
- Functional Amyloids Are the Rule Rather Than the Exception in Cellular Biology.Microorganisms · 2020Review
- SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids.mSystems · 2020Review
- Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells.mBio · 2020Article
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Revised role for Hfq bacterial regulator on DNA topology.Scientific reports · 2018Article
- Handcuffing reversal is facilitated by proteases and replication initiator monomers.Nucleic acids research · 2017Article
- Article
- Outlining Core Pathways of Amyloid Toxicity in Bacteria with the RepA-WH1 Prionoid.Frontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA replication is tightly regulated to constrain the genetic material within strict spatiotemporal boundaries and copy numbers. Bacterial plasmids are autonomously replicating DNA molecules of much clinical, environmental and biotechnological interest. A mechanism used by plasmids to prevent over-replication is 'handcuffing', i.e. inactivating the replication origins in two DNA molecules by holding them together through a bridge built by a plasmid-encoded initiator protein (Rep). Besides being involved in handcuffing, the WH1 domain in the RepA protein assembles as amyloid fibres upon binding to DNA in vitro. The amyloid state in proteins is linked to specific human diseases, but determines selectable and epigenetically transmissible phenotypes in microorganisms. Here we have explored the connection between handcuffing and amyloidogenesis of full-length RepA. Using a monoclonal antibody specific for an amyloidogenic conformation of RepA-WH1, we have found that the handcuffed RepA assemblies, either reconstructed in vitro or in plasmids clustering at the bacterial nucleoid, are amyloidogenic. The replication-inhibitory RepA handcuff assembly is, to our knowledge, the first protein amyloid directly dealing with DNA. Built on an amyloid scaffold, bacterial plasmid handcuffs can bring a novel molecular solution to the universal problem of keeping control on DNA replication initiation.
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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.