Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein

• Ricarda Richter ; Silke Oeljeklaus ; Isotta Lorenzi ^[1]
  1. [1] University Medical Centre Göttingen
• Localización: Cell, ISSN 0092-8674, Vol. 167, Nº. 2, 2016, págs. 471-483
• Idioma: inglés
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• Resumen

  • 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.