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

Holger Webert, Sven-Andreas Freibert, Angelo Gallo, Torsten Heidenreich, Uwe Linne, Stefan Amlacher, Ed Hurt, Ulrich Mühlenhoff, Lucia Banci and Roland Lill ()
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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
Roland Lill: Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6013

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