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Bacterial chaperones CsgE and CsgC differentially modulate human α-Synuclein amyloid formation via transient contacts
E. Chorell, E. Andersson, M.L. Evans, , A. Götheson, J. Aden, M.R. Chapman, F. Almqvist, P. Wittung-Stafshede
Published in Public Library of Science
PMID: 26465894
Volume: 10
Issue: 10
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. © Copyright: 2015 Chorell et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
About the journal
JournalPLoS ONE
PublisherPublic Library of Science