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Título

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

AutorFernández, Cristina; Giraldo, R.
Palabras claveDnaK-DnaJ-GrpE chaperones
RepA-WH1
Cell-free synthetic biology
Giant vesicles
Prion-like protein
Fecha de publicación22-ago-2018
EditorAmerican Chemical Society
CitaciónACS Synth Biol (2018)
ResumenThe 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.
Descripción25 p.-6 fig.
Versión del editorhttps://doi.org/10.1021/acssynbio.8b00283
URIhttp://hdl.handle.net/10261/169388
DOI10.1021/acssynbio.8b00283
E-ISSN2161-5063
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