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  Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I

Kmita, K., Wirth, C., Warnau, J., Guerrero-Castillo, S., Hunte, C., Hummer, G., et al. (2015). Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I. Proceedings of the National Academy of Sciences of the United States of America, 112(18), 5685-5690. doi:10.1073/pnas.1424353112.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-47EA-8 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-922E-D
Genre: Journal Article

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 Creators:
Kmita, Katarzyna1, Author
Wirth, Christophe2, Author
Warnau, Judith3, Author           
Guerrero-Castillo, Sergio4, 5, Author
Hunte, Carola2, Author
Hummer, Gerhard3, Author                 
Kaila, Ville R.I. 6, Author
Zwicker, Klaus7, Author
Brandt, Ulrich4, 5, Author
Zickermann, Volker1, 5, Author
Affiliations:
1Structural Bioenergetics Group, Institute of Biochemistry II, Medical School, Goethe University, 60438 Frankfurt am Main, Germany, ou_persistent22              
2Institute for Biochemistry and Molecular Biology, ZBMZ, BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg Germany, ou_persistent22              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4Nijmegen Center for Mitochondrial Disorders, Radboud University Medical Center, 6525 GA Nijmegen, The Netherlands, ou_persistent22              
5Cluster of Excellence Frankfurt “Macromolecular Complexes”, Goethe University, 60438 Frankfurt am Main, Germany, ou_persistent22              
6Department Chemie, Technische Universität München, 85747 Garching, Germany, ou_persistent22              
7Institute of Biochemistry I, Medical School, Goethe University, 60590 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: Assembly; metal protein; FeS cluster; NDUFAF2; NDUFA12
 Abstract: Mitochondrial proton-pumping NADH:ubiquinone oxidoreductase (respiratory complex I) comprises more than 40 polypeptides and contains eight canonical FeS clusters. The integration of subunits and insertion of cofactors into the nascent complex is a complicated multistep process that is aided by assembly factors. We show that the accessory NUMM subunit of complex I (human NDUFS6) harbors a Zn-binding site and resolve its position by X-ray crystallography. Chromosomal deletion of the NUMM gene or mutation of Zn-binding residues blocked a late step of complex I assembly. An accumulating assembly intermediate lacked accessory subunit N7BM (NDUFA12), whereas a paralog of this subunit, the assembly factor N7BML (NDUFAF2), was found firmly bound instead. EPR spectroscopic analysis and metal content determination after chromatographic purification of the assembly intermediate showed that NUMM is required for insertion or stabilization of FeS cluster N4.

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Language(s): eng - English
 Dates: 2014-12-192015-03-112015-04-202015-05-05
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1424353112
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 112 (18) Sequence Number: - Start / End Page: 5685 - 5690 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230