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Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin

Author

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  • Holger Webert

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg)

  • Sven-Andreas Freibert

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg)

  • Angelo Gallo

    (CERM, Magnetic Resonance Center, University of Florence, Sesto Fiorentino, 50019)

  • Torsten Heidenreich

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg)

  • Uwe Linne

    (Fachbereich Chemie, Philipps-Universität Marburg)

  • Stefan Amlacher

    (Biochemie-Zentrum Heidelberg (BZH))

  • Ed Hurt

    (Biochemie-Zentrum Heidelberg (BZH))

  • Ulrich Mühlenhoff

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg)

  • Lucia Banci

    (CERM, Magnetic Resonance Center, University of Florence, Sesto Fiorentino, 50019
    University of Florence, Via della Lastruccia 3, Sesto Fiorentino, 50019 Florence, Italy)

  • Roland Lill

    (Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg
    Max-Planck-Institut für terrestrische Mikrobiologie
    LOEWE Zentrum für Synthetische Mikrobiologie SynMikro)

Abstract

Maturation of iron–sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe–2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and its reductase Arh1. The roles of Yah1–Arh1 have remained enigmatic, because they are not required for in vitro Fe/S cluster assembly. Here, we reconstitute [2Fe–2S] cluster synthesis on Isu1 in a reaction depending on Nfs1-Isd11, frataxin, Yah1, Arh1 and NADPH. Unlike in the bacterial system, frataxin is an essential part of Fe/S cluster biosynthesis and is required simultaneously and stoichiometrically to Yah1. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1–apo-Isu1. Nuclear magnetic resonance structural studies identify the Yah1–apo-Isu1 interaction surface and suggest a pathway for electron flow from reduced ferredoxin to Isu1. Together, our study defines the molecular function of the ferredoxin Yah1 and its human orthologue FDX2 in mitochondrial Fe/S cluster synthesis.

Suggested Citation

  • Holger Webert & Sven-Andreas Freibert & Angelo Gallo & Torsten Heidenreich & Uwe Linne & Stefan Amlacher & Ed Hurt & Ulrich Mühlenhoff & Lucia Banci & Roland Lill, 2014. "Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6013
    DOI: 10.1038/ncomms6013
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    Cited by:

    1. Vinzent Schulz & Ralf Steinhilper & Jonathan Oltmanns & Sven-A. Freibert & Nils Krapoth & Uwe Linne & Sonja Welsch & Maren H. Hoock & Volker Schünemann & Bonnie J. Murphy & Roland Lill, 2024. "Mechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Sven-A. Freibert & Michal T. Boniecki & Claudia Stümpfig & Vinzent Schulz & Nils Krapoth & Dennis R. Winge & Ulrich Mühlenhoff & Oliver Stehling & Miroslaw Cygler & Roland Lill, 2021. "N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

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