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Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 10, 1-11 p., e0140194Article in journal (Refereed) Published
Abstract [en]

Amyloid formation is historically associated with cytotoxicity, but many organisms produce functional amyloid fibers (e.g., curli) as a normal part of cell biology. Two E. coli genes in the curli operon encode the chaperone-like proteins CsgC and CsgE that both can reduce in vitro amyloid formation by CsgA. CsgC was also found to arrest amyloid formation of the human amyloidogenic protein α-synuclein, which is involved in Parkinson’s disease. Here, we report that the inhibitory effects of CsgC arise due to transient interactions that promote the formation of spherical α-synuclein oligomers. We find that CsgE also modulates α-synuclein amyloid formation through transient contacts but, in contrast to CsgC, CsgE accelerates α-synuclein amyloid formation. Our results demonstrate the significance of transient protein interactions in amyloid regulation and emphasize that the same protein may inhibit one type of amyloid while accelerating another.

Place, publisher, year, edition, pages
2015. Vol. 10, no 10, 1-11 p., e0140194
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Chemical Sciences
URN: urn:nbn:se:umu:diva-110343DOI: 10.1371/journal.pone.0140194ISI: 000363183100087PubMedID: 26465894OAI: diva2:862257
Available from: 2015-10-21 Created: 2015-10-21 Last updated: 2015-11-23Bibliographically approved

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Chorell, ErikAndersson, EmmaGötheson, AnnaÅden, JörgenAlmqvist, FredrikWittung-Stafshede, Pernilla
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Department of ChemistryUmeå Centre for Microbial Research (UCMR)
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