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  The heme a synthase Cox15 associates with cytochrome c oxidase assembly intermediates during Cox1 maturation.

Bareth, B., Dennerlein, S., Mick, D. U., Nikolov, M., Urlaub, H., & Rehling, P. (2013). The heme a synthase Cox15 associates with cytochrome c oxidase assembly intermediates during Cox1 maturation. Molecular and Cellular Biology, 33(20), 4128-4137. doi:10.1128/MCB.00747-13.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-795B-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-BCF2-3
Genre: Journal Article

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 Creators:
Bareth, B., Author
Dennerlein, S., Author
Mick, D. U., Author
Nikolov, M.1, Author              
Urlaub, H.1, Author              
Rehling, P.2, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
2Max Planck Fellow Peter Rehling, ou_1298545              

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 Abstract: Cox1, the core subunit of the cytochrome c oxidase, receives two heme a cofactors during assembly of the 13-subunit enzyme complex. However, at which step of the assembly process and how heme is inserted into Cox1 have remained an enigma. Shy1, the yeast SURF1 homolog, has been implicated in heme transfer to Cox1, whereas the heme a synthase, Cox15, catalyzes the final step of heme a synthesis. Here we performed a comprehensive analysis of cytochrome c oxidase assembly intermediates containing Shy1. Our analyses suggest that Cox15 displays a role in cytochrome c oxidase assembly, which is independent of its functions as the heme a synthase. Cox15 forms protein complexes with Shy1 and also associates with Cox1-containing complexes independently of Shy1 function. These findings indicate that Shy1 does not serve as a mobile heme carrier between the heme a synthase and maturing Cox1 but rather cooperates with Cox15 for heme transfer and insertion in early assembly intermediates of cytochrome c oxidase.

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Language(s): eng - English
 Dates: 2013-08-262013-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1128/MCB.00747-13
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Title: Molecular and Cellular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 33 (20) Sequence Number: - Start / End Page: 4128 - 4137 Identifier: -