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Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts.

Erik Chorell ; Emma Andersson ; Margery L Evans ; Neha Jain ; Anna Götheson ; Jörgen Åden ; Matthew R Chapman ; Fredrik Almqvist ; Pernilla Wittung-Stafshede (Institutionen för biologi och bioteknik, Kemisk biologi)
PloS one (1932-6203). Vol. 10 (2015), 10, p. e0140194.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: Animals, Escherichia coli Proteins, metabolism, Humans, Membrane Transport Proteins, metabolism, Mice, Molecular Chaperones, metabolism, Nuclear Magnetic Resonance, Biomolecular, Protein Aggregation, Pathological, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Recombinant Fusion Proteins, genetics, metabolism, alpha-Synuclein, chemistry, genetics, metabolism



Denna post skapades 2016-12-22. Senast ändrad 2017-10-03.
CPL Pubid: 246467

 

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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Kemisk biologi

Ämnesområden

Biologiska vetenskaper
Biofysik

Chalmers infrastruktur