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  Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I)

Burschel, S., Kreuzer Decovic, D., Nuber, F., Stiller, M., Hofmann, M., Zupok, A., et al. (2019). Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Molecular Microbiology, 111(1), 31-45. doi:10.1111/mmi.14137.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-1109-E Version Permalink: http://hdl.handle.net/21.11116/0000-0005-110A-D
Genre: Journal Article

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Burschel, Sabrina1, Author
Kreuzer Decovic, Doris1, Author
Nuber, Franziska1, Author
Stiller, Marie1, Author
Hofmann, Maud1, Author
Zupok, Arkadiusz1, Author
Siemiatkowska, B.2, Author              
Gorka, M.2, Author              
Leimkühler, Silke1, Author
Friedrich, Thorsten1, Author
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1External Organizations, ou_persistent22              
2Plant Proteomics, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1950285              

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 Abstract: Summary The NADH:ubiquinone oxidoreductase (respiratory complex I) is the main entry point for electrons into the Escherichia coli aerobic respiratory chain. With its sophisticated setup of 13 different subunits and 10 cofactors, it is anticipated that various chaperones are needed for its proper maturation. However, very little is known about the assembly of E. coli complex I, especially concerning the incorporation of the iron-sulfur clusters. To identify iron-sulfur cluster carrier proteins possibly involved in the process, we generated knockout strains of NfuA, BolA, YajL, Mrp, GrxD and IbaG that have been reported either to be involved in the maturation of mitochondrial complex I or to exert influence on the clusters of bacterial complex. We determined the NADH and succinate oxidase activities of membranes from the mutant strains to monitor the specificity of the individual mutations for complex I. The deletion of NfuA, BolA and Mrp led to a decreased stability and partially disturbed assembly of the complex as determined by sucrose gradient centrifugation and native PAGE. EPR spectroscopy of cytoplasmic membranes revealed that the BolA deletion results in the loss of the binuclear Fe/S cluster N1b.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
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 Identifiers: DOI: 10.1111/mmi.14137
BibTex Citekey: doi:10.1111/mmi.14137
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Title: Molecular Microbiology
Source Genre: Journal
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Pages: - Volume / Issue: 111 (1) Sequence Number: - Start / End Page: 31 - 45 Identifier: -