Biology

A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

S. Tiwari, B. Fauvet, et al.

Explore the intriguing mechanism by which Hsp70 chaperones prevent protein aggregation, featuring the novel reporter chaperone substrate MLucV. This research conducted by Satyam Tiwari, Bruno Fauvet, Salvatore Assenza, Paolo De Los Rios, and Pierre Goloubinoff reveals how ATP-fueled actions lead to native MLucV accumulation, even under extreme denaturing conditions!

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Abstract

The mechanism by which Hsp70 chaperones prevent protein aggregation is poorly understood due to the heterogeneity of aggregates. This study designed a reporter chaperone substrate, MLucV, consisting of a stress-labile luciferase flanked by stress-resistant fluorescent domains. Upon denaturation, MLucV formed a discrete population of small aggregates. Using FRET and enzymatic activity, the study characterized MLucV conformations in various states. The Hsp70 mechanism involved ATP-fueled disaggregation and unfolding of the pre-aggregated substrate, extending beyond simple unfolding, followed by refolding. This ATP-fueled action accumulated native MLucV even under highly denaturing conditions, excluding a simple binding-and-prevention mechanism.

Publisher

Nature Chemical Biology

Published On

Oct 20, 2022

Authors

Satyam Tiwari, Bruno Fauvet, Salvatore Assenza, Paolo De Los Rios, Pierre Goloubinoff

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