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Molecular and Cellular Biology, March 2008, p. 1851-1861, Vol. 28, No. 5
0270-7306/08/$08.00+0     doi:10.1128/MCB.01963-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Mitochondrial Iba57p Is Required for Fe/S Cluster Formation on Aconitase and Activation of Radical SAM Enzymes{triangledown} ,{dagger}

Cristy Gelling,1 Ian W. Dawes,1 Nadine Richhardt,2 Roland Lill,2* and Ulrich Mühlenhoff2

School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia,1 Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Str. 6, 35032 Marburg, Germany2

Received 31 October 2007/ Returned for modification 26 November 2007/ Accepted 17 December 2007

A genome-wide screen for Saccharomyces cerevisiae iron-sulfur (Fe/S) cluster assembly mutants identified the gene IBA57. The encoded protein Iba57p is located in the mitochondrial matrix and is essential for mitochondrial DNA maintenance. The growth phenotypes of an iba57{Delta} mutant and extensive functional studies in vivo and in vitro indicate a specific role for Iba57p in the maturation of mitochondrial aconitase-type and radical SAM Fe/S proteins (biotin and lipoic acid synthases). Maturation of other Fe/S proteins occurred normally in the absence of Iba57p. These observations identify Iba57p as a novel dedicated maturation factor with specificity for a subset of Fe/S proteins. The Iba57p primary sequence is distinct from any known Fe/S assembly factor but is similar to certain tetrahydrofolate-binding enzymes, adding a surprising new function to this protein family. Iba57p physically interacts with the mitochondrial ISC assembly components Isa1p and Isa2p. Since all three proteins are conserved in eukaryotes and bacteria, the specificity of the Iba57/Isa complex may represent a biosynthetic concept that is universally used in nature. In keeping with this idea, the human IBA57 homolog C1orf69 complements the iba57{Delta} growth defects, demonstrating its conserved function throughout the eukaryotic kingdom.

* Corresponding author. Mailing address: Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch Str. 6, 35032 Marburg, Germany. Phone: 49-6421-286 6449. Fax: 49-6421-286 6414. E-mail: Lill{at}staff.uni-marburg.de

{triangledown} Published ahead of print on 17 December 2007.

{dagger} We dedicate this paper to the memory of our colleague Ron A. Butow (Dallas, TX).

Molecular and Cellular Biology, March 2008, p. 1851-1861, Vol. 28, No. 5
0270-7306/08/$08.00+0     doi:10.1128/MCB.01963-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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