[摘要]：The chaperonin GroEL plays an essential role in promoting protein folding and in protecting against misfolding and aggregation in the cellular environment. In this study, we report that both GroEL and its isolated apical domain form amyloid-like fibrils under physiological conditions, and that the fibrillation of the apical domain is accelerated under acidic conditions. We also found, however, that despite its fibrillation propensity, the apical domain exhibits a pronounced inhibitory effect on the fibril growth of beta(2)-microglobulin. Thus, the analysis of the behaviour of the apical domain reveals how aggregation and chaperone-mediated anti-aggregation processes can be closely related. Structured summary of protein interactions: groEL and groEL bind by circular dichroism (View interaction) beta 2m and beta 2m bind by transmission electron microscopy (View interaction) beta 2m and beta 2m bind by fluorescence technology (View interaction) groEL and groEL bind by transmission electron microscopy (View interaction) groEL and groEL bind by nuclear magnetic resonance (View interaction) groEL and groEL bind by fluorescence technology (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
