Mitochondrial heat shock protein (hsp) 70 and hsp10 cooperate in the formation of hsp60 complexes
18.03.2015
Böttinger L, Oeljeklaus S, Guiard B, Rospert S, Warscheid B, Becker T.
J Biol Chem. 2015 May 1;290(18):11611-22.
Mitochondrial chaperones are crucial for protein import and folding. The main chaperones of the mitochondrial matrix are the heat shock protein 70 (Hsp70) and Hsp60. Hsp60 forms tetradecameric complexes, which are composed of two rings of Hsp60. These complexes provide chambers for the folding of clients proteins. The co-chaperone Hsp10 forms a lid that close the chamber and stimulates protein folding. How the Hsp60 complexes are formed is poorly understood. We identified an interaction between Hsp70 and Hsp10. This Hsp70-Hsp10 complex promotes the assembly of monomeric Hsp60 precursor into the Hsp60 complexes. We conclude that Hsp70 is recruited to function in Hsp60 complex formation by its interaction with Hsp10.
