Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.

The Journal of Biological Chemistry
Lena BöttingerThomas Becker

Abstract

Mitochondrial Hsp70 (mtHsp70) mediates essential functions for mitochondrial biogenesis, like import and folding of proteins. In these processes, the chaperone cooperates with cochaperones, the presequence translocase, and other chaperone systems. The chaperonin Hsp60, together with its cofactor Hsp10, catalyzes folding of a subset of mtHsp70 client proteins. Hsp60 forms heptameric ring structures that provide a cavity for protein folding. How the Hsp60 rings are assembled is poorly understood. In a comprehensive interaction study, we found that mtHsp70 associates with Hsp60 and Hsp10. Surprisingly, mtHsp70 interacts with Hsp10 independently of Hsp60. The mtHsp70-Hsp10 complex binds to the unassembled Hsp60 precursor to promote its assembly into mature Hsp60 complexes. We conclude that coupling to Hsp10 recruits mtHsp70 to mediate the biogenesis of the heptameric Hsp60 rings.

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Citations

Apr 9, 2016·Cell Stress & Chaperones·Renu WadhwaSunil C Kaul
Jun 17, 2016·Molecular Biology of the Cell·Petri-Jaan LahtveeJens Nielsen
Aug 19, 2016·Mitochondrion·Humberto Gonczarowska-JorgeAlbert Sickmann
Aug 24, 2016·Molecular and Cellular Biology·Isotta LorenziSven Dennerlein
Jun 1, 2018·Journal of Molecular Endocrinology·Hyon-Seung YiMinho Shong
Oct 12, 2018·Journal of Molecular Endocrinology·Hyon-Seung YiMinho Shong
May 15, 2018·Frontiers in Endocrinology·José Pedro CastroAndré Kleinridders
Oct 24, 2020·Nature Reviews. Molecular Cell Biology·Jiyao SongThomas Becker
Apr 4, 2021·International Journal of Molecular Sciences·Masaki KobayashiYoshikazu Higami
Sep 29, 2020·Developmental and Comparative Immunology·Wisarut JunprungAnchalee Tassanakajon
Oct 30, 2021·Frontiers in Molecular Biosciences·Li-Rong YanQian Xu

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