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  MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome-nascent chain complex.

Wang, C., Richter-Dennerlein, R., Pacheu-Grau, D., Liu, F., Zhu, Y., Dennerlein, S., et al. (2019). MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome-nascent chain complex. EMBO Reports, 20(19): e48833. doi:10.15252/embr.201948833.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-4504-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-4509-4
Genre: Journal Article

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3179104.pdf (Publisher version), 2MB
 
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 Creators:
Wang, C., Author
Richter-Dennerlein, R., Author
Pacheu-Grau, D., Author
Liu, F., Author
Zhu, Y., Author
Dennerlein, S., Author
Rehling, P.1, Author              
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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 Abstract: The mitochondrial genome encodes for thirteen core subunits of the oxidative phosphorylation system. These proteins assemble with imported proteins in a modular manner into stoichiometric enzyme complexes. Assembly factors assist in these biogenesis processes by providing co-factors or stabilizing transient assembly stages. However, how expression of the mitochondrial-encoded subunits is regulated to match the availability of nuclear-encoded subunits is still unresolved. Here, we address the function of MITRAC15/COA1, a protein that participates in complex I biogenesis and complex IV biogenesis. Our analyses of a MITRAC15 knockout mutant reveal that MITRAC15 is required for translation of the mitochondrial-encoded complex I subunit ND2. We find that MITRAC15 is a constituent of a ribosome-nascent chain complex during ND2 translation. Chemical crosslinking analyses demonstrate that binding of the ND2-specific assembly factor ACAD9 to the ND2 polypeptide occurs at the C-terminus and thus downstream of MITRAC15. Our analyses demonstrate that expression of the founder subunit ND2 of complex I undergoes regulation. Moreover, a ribosome-nascent chain complex with MITRAC15 is at the heart of this process.

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Language(s): eng - English
 Dates: 2019-11-13
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.15252/embr.201948833
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Title: EMBO Reports
Source Genre: Journal
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Pages: 12 Volume / Issue: 20 (19) Sequence Number: e48833 Start / End Page: - Identifier: -