The iron–sulphur protein Ind1 is required for effective complex I assembly

Bych, Katrine, Kerscher, Stefan, Netz, Daili J. A., Pierik, Antonio J., Zwicker, Klaus, Huynen, Martijn A., Lill, Roland, Brandt, Ulrich and Balk, Janneke (2008) The iron–sulphur protein Ind1 is required for effective complex I assembly. The EMBO Journal, 27 (12). pp. 1736-1746. ISSN 0261-4189

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NADH:ubiquinone oxidoreductase (complex I) of the mitochondrial inner membrane is a multi-subunit protein complex containing eight iron–sulphur (Fe–S) clusters. Little is known about the assembly of complex I and its Fe–S clusters. Here, we report the identification of a mitochondrial protein with a nucleotide-binding domain, named Ind1, that is required specifically for the effective assembly of complex I. Deletion of the IND1 open reading frame in the yeast Yarrowia lipolytica carrying an internal alternative NADH dehydrogenase resulted in slower growth and strongly decreased complex I activity, whereas the activities of other mitochondrial Fe–S enzymes, including aconitase and succinate dehydrogenase, were not affected. Two-dimensional gel electrophoresis, in vitro activity tests and electron paramagnetic resonance signals of Fe–S clusters showed that only a minor fraction (20%) of complex I was assembled in the ind1 deletion mutant. Using in vivo and in vitro approaches, we found that Ind1 can bind a [4Fe–4S] cluster that was readily transferred to an acceptor Fe–S protein. Our data suggest that Ind1 facilitates the assembly of Fe–S cofactors and subunits of complex I.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Groups > Plant Sciences
Depositing User: Rhiannon Harvey
Date Deposited: 01 Feb 2012 10:26
Last Modified: 23 Oct 2022 05:41
DOI: 10.1038/emboj.2008.98

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