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  MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation.

Mick, D. U., Dennerlein, S., Wiese, H., Reinhold, R., Pacheu-Grau, D., Lorenzi, I., et al. (2012). MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation. Cell, 151(7), 1528-1541. doi:10.1016/j.cell.2012.11.053.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-DDDF-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DBD4-D
Genre: Journal Article

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 Creators:
Mick, D. U., Author
Dennerlein, S., Author
Wiese, H., Author
Reinhold, R., Author
Pacheu-Grau, D., Author
Lorenzi, I., Author
Sasarman, F., Author
Weraarpachai, W., Author
Shoubridge, E. A., Author
Warscheid, B., Author
Rehling, P.1, Author              
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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 Abstract: Mitochondrial respiratory-chain complexes assemble from subunits of dual genetic origin assisted by specialized assembly factors. Whereas core subunits are translated on mitochondrial ribosomes, others are imported after cytosolic translation. How imported subunits are ushered to assembly intermediates containing mitochondria-encoded subunits is unresolved. Here,wereport a comprehensive dissection of early cytochromec oxidase assembly intermediates containing proteins required for normal mitochondrial translation and reveal assembly factors promoting biogenesis of human respiratory-chain complexes. We find that TIM21, a subunit of the inner-membrane presequence translocase, is also present in the major assembly intermediates containing newly mitochondria-synthesized and imported respiratory-chain subunits, which we term MITRAC complexes. Human TIM21 is dispensable for protein import but required for integration of early-assembling, presequence-containing subunits into respiratory- chain intermediates. We establish an unexpected molecular link between the TIM23 transport machinery and assembly of respiratory-chain complexes that regulate mitochondrial protein synthesis in response to their assembly state.

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Language(s): eng - English
 Dates: 2012
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2012.11.053
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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 151 (7) Sequence Number: - Start / End Page: 1528 - 1541 Identifier: ISSN: 0092-8674
CoNE: /journals/resource/954925463183