Unknown

Dataset Information

0

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


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.

SUBMITTER: Richter-Dennerlein R 

PROVIDER: S-EPMC5055049 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 facto  ...[more]

Similar Datasets

| S-EPMC4599003 | biostudies-literature
| S-EPMC3625393 | biostudies-literature
2024-03-11 | GSE193134 | GEO
2010-05-27 | E-GEOD-21189 | biostudies-arrayexpress
| S-EPMC6512917 | biostudies-literature
| S-EPMC3904643 | biostudies-literature
| S-EPMC2764937 | biostudies-literature