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dc.contributor.authorTorreira, Evaes_ES
dc.contributor.authorMoreno-del Álamo, Maríaes_ES
dc.contributor.authorFuentes-Perez, M. E.es_ES
dc.contributor.authorFernández, Cristinaes_ES
dc.contributor.authorMartín-Benito, Jaimees_ES
dc.contributor.authorMoreno-Herrero, Fernandoes_ES
dc.contributor.authorGiraldo, R.es_ES
dc.contributor.authorLlorca, Óscares_ES
dc.date.accessioned2015-08-06T14:40:38Z-
dc.date.available2015-08-06T14:40:38Z-
dc.date.issued2015-01-06-
dc.identifier.citationStructure 23: 183–189 (2015)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/121034-
dc.description.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.es_ES
dc.description.sponsorshipThis work was supported by grants of the Spanish Government SAF2011- 22988 and the Autonomous Region of Madrid S2010/BMD-2316 to O.L.; BIO2012-30852 and CSD2009-00088 to R.G.; BFU2011-25090 to J.M.-B.; and FIS2011-24638 and ERC Starting grant ref 206117 to F.M.-H.es_ES
dc.language.isoenges_ES
dc.publisherNature Publishing Groupes_ES
dc.relation206117 FP7-IDEAS-ERCes_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccesses_ES
dc.subjectamyloid proteines_ES
dc.subjectbacterial proteines_ES
dc.subjectDNA helicasees_ES
dc.subjectRepA WH1 proteines_ES
dc.titleAmyloidogenesis of bacterial prionoid RepA-WH1 recapitulates dimer to monomer transitions of RepA in DNA replication initiation.es_ES
dc.title.alternativeStructure of RepA-WH1 amyloid filamentses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.str.2014.11.007-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.str.2014.11.007es_ES
dc.identifier.e-issn0969-2126-
dc.contributor.funderEuropean Commissiones_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderComunidad de Madrides_ES
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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