Prohibitins Interact Genetically with Atp23, a Novel Processing Peptidase and Chaperone for the F1FO-ATP Synthase

• DOI: 10.1091/mbc.e06-09-0839
• Publication Date: 2006-11-30T01:40:08Z
• Authors: Christof Osman; Claudia Wilmes; Takashi Tatsuta; Thomas Langer
• Keywords: Chaperone (clinical)

The generation of cellular energy depends on the coordinated assembly nuclear and mitochondrial-encoded proteins into multisubunit respiratory chain complexes in inner membrane mitochondria. Here, we describe identification a conserved metallopeptidase present intermembrane space, termed Atp23, which exerts dual activities during biogenesis F(1)F(O)-ATP synthase. On one hand, Atp23 serves as processing peptidase mediates maturation F(O)-subunit Atp6 after its insertion membrane. other hand independent proteolytic activity, promotes association mature with Atp9 oligomers. This step is thus under control two substrate-specific chaperones, Atp10 act opposite sides Strikingly, both ATP10 ATP23 were found to genetically interact prohibitins, build up large, ring-like assemblies proposed scaffolding function Our results therefore characterize not only novel chaperone activity mitochondrial space but also link prohibitins synthase complex.