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Cell. 2016 Oct 6;167(2):471-483.e10. doi: 10.1016/j.cell.2016.09.003. Epub 2016 Sep 29.

Mitochondrial Protein Synthesis Adapts to Influx of Nuclear-Encoded Protein.

Author information

1
Department of Cellular Biochemistry, University Medical Centre Göttingen, GZMB, 37073 Göttingen, Germany.
2
Department of Biochemistry and Functional Proteomics, Faculty of Biology, University Freiburg, 79104 Freiburg, Germany.
3
Department of Biochemistry and Functional Proteomics, Faculty of Biology, University Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.
4
Department of Cellular Biochemistry, University Medical Centre Göttingen, GZMB, 37073 Göttingen, Germany; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. Electronic address: peter.rehling@medizin.uni-goettingen.de.

Abstract

Mitochondrial ribosomes translate membrane integral core subunits of the oxidative phosphorylation system encoded by mtDNA. These translation products associate with nuclear-encoded, imported proteins to form enzyme complexes that produce ATP. Here, we show that human mitochondrial ribosomes display translational plasticity to cope with the supply of imported nuclear-encoded subunits. Ribosomes expressing mitochondrial-encoded COX1 mRNA selectively engage with cytochrome c oxidase assembly factors in the inner membrane. Assembly defects of the cytochrome c oxidase arrest mitochondrial translation in a ribosome nascent chain complex with a partially membrane-inserted COX1 translation product. This complex represents a primed state of the translation product that can be retrieved for assembly. These findings establish a mammalian translational plasticity pathway in mitochondria that enables adaptation of mitochondrial protein synthesis to the influx of nuclear-encoded subunits.

KEYWORDS:

C12ORF62; COX1; MITRAC; OXPHOS; assembly; cytochrome c oxidase; mitochondrial ribosome; mitochondrial translation; translation regulation; translational plasticity

PMID:
27693358
PMCID:
PMC5055049
DOI:
10.1016/j.cell.2016.09.003
[Indexed for MEDLINE]
Free PMC Article

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