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  Spatial orchestration of mitochondrial translation and OXPHOS complex assembly.

Stoldt, S., Wenzel, D., Kehrein, K., Riedel, D., Ott, M., & Jakobs, S. (2018). Spatial orchestration of mitochondrial translation and OXPHOS complex assembly. Nature Cell Biology, 20(5), 528-534. doi:10.1038/s41556-018-0090-7.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-2EB7-E Version Permalink: http://hdl.handle.net/21.11116/0000-0003-BC0D-C
Genre: Journal Article

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 Creators:
Stoldt, S.1, Author              
Wenzel, D.2, Author              
Kehrein, K., Author
Riedel, D.2, Author              
Ott, M., Author
Jakobs, S.1, Author              
Affiliations:
1Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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 Abstract: Oxidative phosphorylation (OXPHOS) is vital for the regeneration of the vast majority of ATP in eukaryotic cells 1 . OXPHOS is carried out by large multi-subunit protein complexes in the cristae membranes, which are invaginations of the mitochondrial inner membrane. The OXPHOS complexes are a mix of subunits encoded in the nuclear and mitochondrial genomes. Thus, the assembly of these dual-origin complexes is an enormous logistical challenge for the cell. Using super-resolution microscopy (nanoscopy) and quantitative cryo-immunogold electron microscopy, we determined where specific transcripts are translated and where distinct assembly steps of the dual-origin complexes in the yeast Saccharomyces cerevisiae occur. Our data indicate that the mitochondrially encoded proteins of complex III and complex IV are preferentially inserted in different sites of the inner membrane than those of complex V. We further demonstrate that the early, but not the late, assembly steps of complex III and complex IV occur preferentially in the inner boundary membrane. By contrast, all steps of complex V assembly occur mainly in the cristae membranes. Thus, OXPHOS complex assembly is spatially well orchestrated, probably representing an unappreciated regulatory layer in mitochondrial biogenesis.

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Language(s): eng - English
 Dates: 2018-04-162018-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41556-018-0090-7
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Title: Nature Cell Biology
Source Genre: Journal
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Pages: - Volume / Issue: 20 (5) Sequence Number: - Start / End Page: 528 - 534 Identifier: -