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Título

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

Otros títulosStructure of RepA-WH1 amyloid filaments
AutorTorreira, Eva ; Moreno-del Álamo, María ; Fuentes-Perez, M. E.; Fernández, Cristina; Martín-Benito, Jaime; Moreno-Herrero, Fernando; Giraldo, R. ; Llorca, Óscar
Palabras claveamyloid protein
bacterial protein
DNA helicase
RepA WH1 protein
Fecha de publicación6-ene-2015
EditorNature Publishing Group
CitaciónStructure 23: 183–189 (2015)
ResumenMost 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.
Versión del editorhttp://dx.doi.org/10.1016/j.str.2014.11.007
URIhttp://hdl.handle.net/10261/121034
DOI10.1016/j.str.2014.11.007
E-ISSN0969-2126
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