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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
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
Appears in Collections:(CIB) Artículos
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