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Vol. 18, Issue 2, 627-635, February 2007

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Prohibitins Interact Genetically with Atp23, a Novel Processing Peptidase and Chaperone for the F₁F_O-ATP Synthase

Institute for Genetics and Center for Molecular Medicine, University of Cologne, D-50674 Cologne, Germany

Submitted September 19, 2006; Revised November 16, 2006; Accepted November 21, 2006
Monitoring Editor: Thomas Fox

The generation of cellular energy depends on the coordinated assembly of nuclear and mitochondrial-encoded proteins into multisubunit respiratory chain complexes in the inner membrane of mitochondria. Here, we describe the identification of a conserved metallopeptidase present in the intermembrane space, termed Atp23, which exerts dual activities during the biogenesis of the F₁F_O-ATP synthase. On one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrial-encoded F_O-subunit Atp6 after its insertion into the inner membrane. On the other hand and independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers. This assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane. Strikingly, both ATP10 and ATP23 were found to genetically interact with prohibitins, which build up large, ring-like assemblies with a proposed scaffolding function in the inner membrane. Our results therefore characterize not only a novel processing peptidase with chaperone activity in the mitochondrial intermembrane space but also link the function of prohibitins to the F₁F_O-ATP synthase complex.

¹ Similar findings are reported in a related study by Zeng et al. (2007) published in this issue of MBC.

* These authors contributed equally to this work.

Address correspondence to: Thomas Langer (Thomas.Langer{at}uni-koeln.de)

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