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Título: | Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid |
Autor: | Moreno-del Álamo, María CSIC ORCID ; Moreno Díaz de la Espina, Susana CSIC ORCID ; Fernández-Tresguerres, María Elena CSIC ; Giraldo, R. CSIC ORCID | Fecha de publicación: | 1-oct-2015 | Editor: | Nature Publishing Group | Citación: | Scientific Reports 5: 14669 (2015) | Resumen: | Upon binding to short specific dsDNA sequences in vitro, the N-terminal WH1 domain of the plasmid DNA replication initiator RepA assembles as amyloid fibres. These are bundles of single or double twisted tubular filaments in which distorted RepA-WH1 monomers are the building blocks. When expressed in Escherichia coli, RepA-WH1 triggers the first synthetic amyloid proteinopathy in bacteria, recapitulating some of the features of mammalian prion diseases: it is vertically transmissible, albeit non-infectious, showing up in at least two phenotypically distinct and interconvertible strains. Here we report B3h7, a monoclonal antibody specific for oligomers of RepA-WH1, but which does not recognize the mature amyloid fibres. Unlike a control polyclonal antibody generated against the soluble protein, B3h7 interferes in vitro with DNA-promoted or amyloid-seeded assembly of RepA-WH1 fibres, thus the targeted oligomers are on-pathway amyloidogenic intermediates. Immuno-electron microscopy with B3h7 on thin sections of E. coli cells expressing RepA-WH1 consistently labels the bacterial nucleoid, but not the large cytoplasmic aggregates of the protein. This observation points to the nucleoid as the place where oligomeric amyloid precursors of RepA-WH1 are generated, and suggests that, once nucleated by DNA, further growth must continue in the cytoplasm due to entropic exclusion. | Descripción: | 12 p.-4 fig. | Versión del editor: | http://dx.doi.org/ 10.1038/srep14669 | URI: | http://hdl.handle.net/10261/128195 | DOI: | 10.1038/srep14669 | ISSN: | 2045-2322 | E-ISSN: | 2045-2322 |
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srep_Giraldo, R._2015.pdf | Artículo principal | 2,91 MB | Adobe PDF | Visualizar/Abrir |
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