Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging
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...
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doaj-cb1bd9a91ee747db9a872edc60d0d6492020-11-24T23:38:40ZengShared Science Publishers OGMicrobial Cell2311-26382018-01-015419820710.15698/mic2018.04.625Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic agingNadia G Rampello0Maria Stenger1Benedikt Westermann2Heinz D Osiewacz3Department of Biosciences, Molecular Developmental Biology, Institute of Molecular Biosciences and Cluster of Excellence Frankfurt Macromolecular Complexes, J. W. Goethe University, 60438 Frankfurt, Germany.Cell Biology and Electron Microscopy, University of Bayreuth, 95440 Bayreuth, Germany.Cell Biology and Electron Microscopy, University of Bayreuth, 95440 Bayreuth, Germany.Department of Biosciences, Molecular Developmental Biology, Institute of Molecular Biosciences and Cluster of Excellence Frankfurt Macromolecular Complexes, J. W. Goethe University, 60438 Frankfurt, Germany.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.http://microbialcell.com/researcharticles/impact-of-f1fo-atp-synthase-dimer-assembly-factors-on-mitochondrial-function-and-organismic-aging/agingF1Fo-ATP-synthasemembranesmitochondriaremodeling |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nadia G Rampello Maria Stenger Benedikt Westermann Heinz D Osiewacz |
spellingShingle |
Nadia G Rampello Maria Stenger Benedikt Westermann Heinz D Osiewacz Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging Microbial Cell aging F1Fo-ATP-synthase membranes mitochondria remodeling |
author_facet |
Nadia G Rampello Maria Stenger Benedikt Westermann Heinz D Osiewacz |
author_sort |
Nadia G Rampello |
title |
Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging |
title_short |
Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging |
title_full |
Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging |
title_fullStr |
Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging |
title_full_unstemmed |
Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging |
title_sort |
impact of f1fo-atp-synthase dimer assembly factors on mitochondrial function and organismic aging |
publisher |
Shared Science Publishers OG |
series |
Microbial Cell |
issn |
2311-2638 |
publishDate |
2018-01-01 |
description |
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. |
topic |
aging F1Fo-ATP-synthase membranes mitochondria remodeling |
url |
http://microbialcell.com/researcharticles/impact-of-f1fo-atp-synthase-dimer-assembly-factors-on-mitochondrial-function-and-organismic-aging/ |
work_keys_str_mv |
AT nadiagrampello impactoff1foatpsynthasedimerassemblyfactorsonmitochondrialfunctionandorganismicaging AT mariastenger impactoff1foatpsynthasedimerassemblyfactorsonmitochondrialfunctionandorganismicaging AT benediktwestermann impactoff1foatpsynthasedimerassemblyfactorsonmitochondrialfunctionandorganismicaging AT heinzdosiewacz impactoff1foatpsynthasedimerassemblyfactorsonmitochondrialfunctionandorganismicaging |
_version_ |
1725516287476498432 |