Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging

Authors:

Nadia G Rampello1, Maria Stenger2, Benedikt Westermann2, Heinz D Osiewacz1

doi: 10.15698/mic2018.04.625
Volume 5, pp. 198 to 207, published 30/01/2018.

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Affiliations:

1 Department of Biosciences, Molecular Developmental Biology, Institute of Molecular Biosciences and Cluster of Excellence Frankfurt Macromolecular Complexes, J. W. Goethe University, 60438 Frankfurt, Germany.

2 Cell Biology and Electron Microscopy, University of Bayreuth, 95440 Bayreuth, Germany.

Keywords: 

aging, F1Fo-ATP-synthase, membranes, mitochondria, remodeling

Corresponding Author(s):

Heinz D. Osiewacz, Tel: +496979829264; Osiewacz@bio.uni-frankfurt.de

Conflict of interest statement:

The authors declare that they have no conflict of interest.

Please cite this article as:

Nadia G Rampello, Maria Stenger, Benedikt Westermann, Heinz D Osiewacz (2018). Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging. Microbial Cell 5(4): 198-207. doi: 10.15698/mic2018.04.625

© 2018 Rampello et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

Abstract:

In aerobic organisms, mitochondrial F1Fo-ATP-synthase is the major site of ATP production. Beside this fundamental role, the protein complex is involved in shaping and maintenance of cristae. Previous electron microscopic studies identified the dissociation of F1Fo-ATP-synthase dimers and oligomers during organismic aging correlating with a massive remodeling of the mitochondrial inner membrane. Here we report results aimed to experimentally proof this impact and to obtain further insights into the control of these processes. We focused on the role of the two dimer assembly factors PaATPE and PaATPG of the aging model Podospora anserina. Ablation of either protein strongly affects mitochondrial function and leads to an accumulation of senescence markers demonstrating that the inhibition of dimer formation negatively influences vital functions and accelerates organismic aging. Our data validate a model that links mitochondrial membrane remodeling to aging and identify specific molecular components triggering this process.