Cristae architecture is determined by an interplay of the MICOS complex and the F1Fo ATP synthase via Mic27 and Mic10
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.
- Authors:
-
- Goethe University, Frankfurt (Germany)
- Max Planck Inst. of Biophysics, Frankfurt am Main (Germany); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Heinrich Heine University, Dusseldorf (Germany)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division: German Research Foundation (DFG); Max Planck Society
- OSTI Identifier:
- 1629532
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Microbial Cell
- Additional Journal Information:
- Journal Volume: 4; Journal Issue: 8; Journal ID: ISSN 2311-2638
- Publisher:
- Shared Science Publishers OG
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; membrane structure; bioenergetics; mitochondria; cristae; membrane protein complex; crista junction
Citation Formats
Eydt, Katharina, Davis, Karen M., Behrendt, Christina, Wittig, Ilka, and Reichert, Andreas S. Cristae architecture is determined by an interplay of the MICOS complex and the F1Fo ATP synthase via Mic27 and Mic10. United States: N. p., 2017.
Web. doi:10.15698/mic2017.08.585.
Eydt, Katharina, Davis, Karen M., Behrendt, Christina, Wittig, Ilka, & Reichert, Andreas S. Cristae architecture is determined by an interplay of the MICOS complex and the F1Fo ATP synthase via Mic27 and Mic10. United States. https://doi.org/10.15698/mic2017.08.585
Eydt, Katharina, Davis, Karen M., Behrendt, Christina, Wittig, Ilka, and Reichert, Andreas S. Mon .
"Cristae architecture is determined by an interplay of the MICOS complex and the F1Fo ATP synthase via Mic27 and Mic10". United States. https://doi.org/10.15698/mic2017.08.585. https://www.osti.gov/servlets/purl/1629532.
@article{osti_1629532,
title = {Cristae architecture is determined by an interplay of the MICOS complex and the F1Fo ATP synthase via Mic27 and Mic10},
author = {Eydt, Katharina and Davis, Karen M. and Behrendt, Christina and Wittig, Ilka and Reichert, Andreas S.},
abstractNote = {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.},
doi = {10.15698/mic2017.08.585},
journal = {Microbial Cell},
number = 8,
volume = 4,
place = {United States},
year = {Mon Aug 07 00:00:00 EDT 2017},
month = {Mon Aug 07 00:00:00 EDT 2017}
}
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