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Journal Article

Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein.

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2351809.pdf
(Publisher version), 5MB

Supplementary Material (public)

2351809_Suppl_1.pdf
(Supplementary material), 145KB

2351809_Suppl_2.xlsx
(Supplementary material), 554KB

2351809_Suppl_3.xlsx
(Supplementary material), 11KB

Citation

Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsör, C., Bareth, B., Schendzielorz, A. B., et al. (2016). Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein. Cell, 167(2), 471-483. doi:10.1016/j.cell.2016.09.003.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-9968-2
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.