title: Mitochondrial heat shock protein (Hsp) 70 and Hsp10 cooperate in the formation of Hsp60 complexes.
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.
authors: From the Institut für Biochemie und Molekularbiologie, ZBMZ, the Fakultät für Biologie.
authors: Lena
authors: L
authors: Böttinger
authors: Institut für Biologie II, Abteilung Biochemie und Funktionelle Proteomik, Universität Freiburg, 79104 Freiburg, Germany, the BIOSS Centre for Biological Signalling Studies, and.
authors: Silke
authors: S
authors: Oeljeklaus
authors: the Centre de Génétique Moléculaire, CNRS, 91190 Gif-sur-Yvette, France.
authors: Bernard
authors: B
authors: Guiard
authors: From the Institut für Biochemie und Molekularbiologie, ZBMZ, the BIOSS Centre for Biological Signalling Studies, and.
authors: Sabine
authors: S
authors: Rospert
authors: Institut für Biologie II, Abteilung Biochemie und Funktionelle Proteomik, Universität Freiburg, 79104 Freiburg, Germany, the BIOSS Centre for Biological Signalling Studies, and.
authors: Bettina
authors: B
authors: Warscheid
authors: From the Institut für Biochemie und Molekularbiologie, ZBMZ, the Fakultät für Biologie, the BIOSS Centre for Biological Signalling Studies, and thomas.becker@biochemie.uni-freiburg.de.
authors: Thomas
authors: T
authors: Becker
mesh_terms: D000818:Animals; D018835:Chaperonin 10 / Q000378:metabolism*; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D018840:HSP70 Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins
keywords: 70-kDa Heat Shock Protein (Hsp70); Hsp10; Hsp60; Mitochondria; Molecular Chaperone; Protein Assembly; Protein Biogenesis; Protein Folding