Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone

FEBS Letters
Jin ChenKunihiro Kuwajima

Abstract

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 β(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.

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Citations

Apr 23, 2013·FEBS Letters·Maho Yagi-UtsumiKoichi Kato
Jun 11, 2015·The FEBS Journal·Francesco AngelucciVeronica Morea
Jul 31, 2016·Biochimica Et Biophysica Acta·Maria Rosalia MangionePier Luigi San Biagio
Apr 22, 2017·The Journal of Physical Chemistry. B·Jin ChenWenfei Li
Jun 22, 2021·Frontiers in Bioengineering and Biotechnology·Huifang ZhangHanjie Ying

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