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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-9968-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-0B9E-D
Genre: Journal Article

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 Creators:
Richter-Dennerlein, R., Author
Oeljeklaus, S., Author
Lorenzi, I., Author
Ronsör, C., Author
Bareth, B., Author
Schendzielorz, A. B., Author
Wang, C., Author
Warscheid, B., Author
Rehling, P.1, Author              
Dennerlein, S., Author
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: C12ORF62; COX1; MITRAC; OXPHOS; Asembly; Cytochrome c oxidase; Mitochondrial ribosome; Mitochondrial translation; Translation regulation; Translational plasticity
 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.

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Language(s): eng - English
 Dates: 2016-09-292016-10-06
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2016.09.003
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Title: Cell
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 167 (2) Sequence Number: - Start / End Page: 471 - 483 Identifier: -