Clumped proteins can be dissolved with the aid of cellular repair systems – a process of critical importance for cell survival especially under conditions of stress. Heidelberg researchers have now decrypted the fundamental mechanism for dissolving protein aggregates that involves specific molecular chaperones.
Mechanism of protein aggregate dissolution through Hsp70/Hsp100 cooperation. The ring-shaped Hsp100 has two structural states, one inactive and the other activated. A molecular switch keeps the Hsp100 chaperone in the inactive state. Hsp70 causes the switch to flip, thereby activating the Hsp100 chaperone. In this state it can pull protein strands out of the aggregate. The activation of Hsp100 is not permanent, with the chaperone reverting to the inactive state after the aggregate has dissolved.
Picture credits: ZMBH
Marietta Fuhrmann-Koch | idw
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