English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/169388
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Modulation of the aggregation of the prion-like rotein RepA-WH1 by chaperones in a cell-free expression system and in cytomimetic lipid vesicles

AuthorsFernández, Cristina; Giraldo, R.
KeywordsDnaK-DnaJ-GrpE chaperones
RepA-WH1
Cell-free synthetic biology
Giant vesicles
Prion-like protein
Issue Date21-Sep-2018
PublisherAmerican Chemical Society
CitationACS Synth Biol 7(9):2087-2093 (2018)
AbstractThe accumulation of aggregated forms of proteins as toxic species is associated with fatal diseases such as amyloid proteinopathies. With the purpose of deconstructing the molecular mechanisms of these type of diseases through a Synthetic Biology approach, we are working with a model bacterial prion-like protein, RepA-WH1, expressed in a cell-free system. Our findings show that the Hsp70 chaperone from Escherichia coli, together with its Hsp40 and nucleotide exchange factor cochaperones, modulates the aggregation of the prion-like protein in the cell-free system. Moreover, we observe the same effect by reconstructing the aggregation process inside lipid vesicles. Chaperones reduce the number of aggregates formed, matching previous findings in vivo. We expect that the in vitro approach reported here will help to achieve better understanding and control of amyloid proteinopathies.
Description25 p.-6 fig.
Publisher version (URL)https://doi.org/10.1021/acssynbio.8b00283
URIhttp://hdl.handle.net/10261/169388
DOI10.1021/acssynbio.8b00283
E-ISSN2161-5063
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
Fernandez-Giraldo_ACSSynthBiol2018_final-2.pdf Embargoed until September 21, 2019Postprint8,9 MBAdobe PDFThumbnail
View/Open    Request a copy
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.