Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10

Authors:

Katharina Eydt1,2, Karen M. Davies3, Christina Behrendt4, Ilka Wittig1,5 and Andreas S. Reichert1,2,4,*

doi: 10.15698/mic2017.08.585
Volume 4, pp. 259 to 272, published 20/07/2017.

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Affiliations:

1 Cluster of Excellence Macromolecular Complexes, Goethe University Frankfurt, Max-von-Laue-Str. 15, Frankfurt am Main, Germany.

2 Mitochondrial Biology, Buchmann Institute of Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany.

3 Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany. Present address: Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.

4 Institute of Biochemistry and Molecular Biology I, Medical Faculty Heinrich Heine University, Universitätsstr. 1, 40225 Düsseldorf, Germany.

5 Functional Proteomics, SFB 815 Core Unit, Faculty of Medicine, Goethe University Frankfurt, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.

Keywords: 

membrane structure, bioenergetics, mitochondria, cristae, membrane protein complex, crista junction.

Corresponding Author(s):

Andreas S. Reichert, Tel: +49 21181 12707; Fax: +49 21181 13029; reichert@hhu.de

Conflict of interest statement:

The authors declare that there is no conflict of interest associated with this manuscript.

Please cite this article as:

Please cite this article as: Katharina Eydt, Karen Davies, Christina Behrendt, Ilka Wittig and Andreas S. Reichert (2017). Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10. Microbial Cell 4(8): 259-272. doi: 10.15698/mic2017.08.585

© 2017 Eydt 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:

The inner boundary and the cristae membrane are connected by pore-like structures termed crista junctions (CJs). The MICOS complex is required for CJ formation and enriched at CJs. Here, we address the roles of the MICOS subunits Mic27 and Mic10. We observe a positive genetic interaction between Mic27 and Mic60 and deletion of Mic27 results in impaired formation of CJs and altered cristae membrane curvature. Mic27 acts in an antagonistic manner to Mic60 as it promotes oligomerization of the F1FO-ATP synthase and partially restores CJ formation in cells lacking Mic60. Mic10 impairs oligomerization of the F1FO-ATP synthase similar to Mic60. Applying complexome profiling, we observed that deletion of Mic27 destabilizes the MICOS complex but does not impair formation of a high molecular weight Mic10 subcomplex. Moreover, this Mic10 subcomplex comigrates with the dimeric F1FO-ATP synthase in a Mic27-independent manner. Further, we observed a chemical crosslink of Mic10 to Mic27 and of Mic10 to the F1FO-ATP synthase subunit e. We corroborate the physical interaction of the MICOS complex and the F1FO-ATP synthase. We propose a model in which part of the F1FO-ATP synthase is linked to the MICOS complex via Mic10 and Mic27 and by that is regulating CJ formation.