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Amyloidogenesis of bacterial prionoid RepA-WH1 recapitulates dimer to monomer transitions of RepA in DNA replication initiation.

Other TitlesStructure of RepA-WH1 amyloid filaments
AuthorsTorreira, Eva CSIC; Moreno-del Álamo, María CSIC ORCID ; Fuentes-Perez, M. E.; Fernández, Cristina; Martín-Benito, Jaime; Moreno-Herrero, Fernando; Giraldo, R. CSIC ORCID; Llorca, Óscar
KeywordsAmyloid protein
Bacterial proteins
DNA helicase
RepA WH1 protein
Issue Date6-Jan-2015
PublisherNature Publishing Group
CitationStructure 23: 183–189 (2015)
AbstractMost available structures of amyloids correspond to peptide fragments that self-assemble in extended cross b sheets. However, structures in which a whole protein domain acts as building block of an amyloid fiber are scarce, in spite of their relevance to understand amyloidogenesis. Here, we use electron microscopy (EM) and atomic force microscopy (AFM) to analyze the structure of amyloid filaments assembled by RepA-WH1, a winged-helix domain from a DNA replication initiator in bacterial plasmids. RepA-WH1 functions as a cytotoxic bacterial prionoid that recapitulates features of mammalian amyloid proteinopathies. RepA are dimers that monomerize at the origin to initiate replication, and we find that RepA-WH1 reproduces this transition to form amyloids. RepA-WH1 assembles double helical filaments by lateral association of a singlestranded precursor built by monomers. Double filaments then associate in mature fibers. The intracellular and cytotoxic RepA-WH1 aggregates might reproduce the hierarchical assembly of human amyloidogenic proteins.
Publisher version (URL)http://dx.doi.org/10.1016/j.str.2014.11.007
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