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http://hdl.handle.net/10261/131499
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Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Giraldo, R. | es_ES |
dc.contributor.author | Fernández, Cristina | es_ES |
dc.contributor.author | Moreno-del Álamo, María | es_ES |
dc.contributor.author | Molina-García, Laura | es_ES |
dc.contributor.author | Revilla-García, Aída | es_ES |
dc.contributor.author | Sánchez-Martínez, María Cruz | es_ES |
dc.contributor.author | Giménez-Abián, Juan F. | es_ES |
dc.contributor.author | Moreno Díaz de la Espina, Susana | es_ES |
dc.date.issued | 2016-04-04 | - |
dc.identifier.citation | Prion, 10:41–49 ( 2016) | es_ES |
dc.identifier.issn | 1933-6896 | - |
dc.identifier.uri | http://hdl.handle.net/10261/131499 | - |
dc.description | 10 p.-1 fig. | es_ES |
dc.description.abstract | In bacterial plasmids, Rep proteins initiate DNA replication by undergoing a structural transformation coupled to dimer dissociation. Amyloidogenesis of the ‘winged-helix’ N-terminal domain of RepA (WH1) is triggered in vitro upon binding to plasmid-specific DNA sequences, and occurs at the bacterial nucleoid in vivo. Amyloid fibers are made of distorted RepA-WH1 monomers that assemble as single or double intertwined tubular protofilaments. RepA-WH1 causes in E. coli an amyloid proteinopathy, which is transmissible from mother to daughter cells, but not infectious, and enables conformational imprinting in vitro and in vivo; i.e. RepA-WH1 is a ‘prionoid’. Microfluidics allow the assessment of the intracellular dynamics of RepA-WH1: bacterial lineages maintain two types (strains-like) of RepA-WH1 amyloids, either multiple compact cytotoxic particles or a single aggregate with the appearance of a fluidized hydrogel that it is mildly detrimental to growth. The Hsp70 chaperone DnaK governs the phase transition between both types of RepA-WH1 aggregates in vivo, thus modulating the vertical propagation of the prionoid. Engineering chimeras between the Sup35p/[PSI*] prion and RepA-WH1 generates [REP-PSI*], a synthetic prion exhibiting strong and weak phenotypic variants in yeast. These recent findings on a synthetic, self-contained bacterial prionoid illuminate central issues of protein amyloidogenesis. | es_ES |
dc.description.sponsorship | Research on RepA-WH1 amyloids at CIBCSIC is currently financed by Spanish MINECO grants BIO2012-30852 and CSD2009-00088. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Taylor & Francis | es_ES |
dc.rights | openAccess | es_ES |
dc.subject | Amyloid proteinopathy | es_ES |
dc.subject | Amyloid polymorphism | es_ES |
dc.subject | Bacterial prionoid | es_ES |
dc.subject | Hsp70 chaperone | es_ES |
dc.subject | Phase transitions | es_ES |
dc.subject | RepA-WH1 | es_ES |
dc.title | RepA-WH1 prionoid: Clues from bacteria on factors governing phase transitions in amyloidogenesis | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1080/19336896.2015.1129479 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1080/19336896.2015.1129479 | es_ES |
dc.identifier.e-issn | 1933-690X | - |
dc.rights.license | http://creativecommons.org/licenses/by-nc/3.0/ | es_ES |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | es_ES |
dc.relation.csic | Sí | es_ES |
oprm.item.hasRevision | no ko 0 false | * |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.pmid | 27040981 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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Fichero | Descripción | Tamaño | Formato | |
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Prion_Giraldo_2016.pdf | Artículo principal | 1,08 MB | Adobe PDF | Visualizar/Abrir |
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