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Originally published as MBC in Press, 10.1091/mbc.E05-03-0256 on August 31, 2005

Vol. 16, Issue 11, 5202-5214, November 2005

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Taz1, an Outer Mitochondrial Membrane Protein, Affects Stability and Assembly of Inner Membrane Protein Complexes: Implications for Barth Syndrome

Katrin Brandner * {dagger}, David U. Mick *, Ann E. Frazier * {ddagger}, Rebecca D. Taylor *, Chris Meisinger *, and Peter Rehling *

* Institut für Biochemie und Molekularbiologie, Universität Freiburg, D-79104 Freiburg, Germany; {ddagger} Department of Biochemistry, La Trobe University, 3086 Melbourne, Australia

Submitted March 25, 2005; Revised August 22, 2005; Accepted August 24, 2005
Monitoring Editor: Suresh Subramani

The Saccharomyces cerevisiae Taz1 protein is the orthologue of human Tafazzin, a protein that when inactive causes Barth Syndrome (BTHS), a severe inherited X-linked disease. Taz1 is a mitochondrial acyltransferase involved in the remodeling of cardiolipin. We show that Taz1 is an outer mitochondrial membrane protein exposed to the intermembrane space (IMS). Transport of Taz1 into mitochondria depends on the receptor Tom5 of the translocase of the outer membrane (TOM complex) and the small Tim proteins of the IMS, but is independent of the sorting and assembly complex (SAM). TAZ1 deletion in yeast leads to growth defects on nonfermentable carbon sources, indicative of a defect in respiration. Because cardiolipin has been proposed to stabilize supercomplexes of the respiratory chain complexes III and IV, we assess supercomplexes in taz1{Delta} mitochondria and show that these are destabilized in taz1{Delta} mitochondria. This leads to a selective release of a complex IV monomer from the III2IV2 supercomplex. In addition, assembly analyses of newly imported subunits into complex IV show that incorporation of the complex IV monomer into supercomplexes is affected in taz1{Delta} mitochondria. We conclude that inactivation of Taz1 affects both assembly and stability of respiratory chain complexes in the inner membrane of mitochondria.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–03–0256) on August 31, 2005.

Abbreviations used: AAC, ADP/ATP carrier; BN-PAGE, blue native-PAGE; BTHS, Barth syndrome; {Delta}{psi}, membrane potential.

{dagger} Present address: Institut de Biologie Moléculaire des Plantes, CNRS UPR 2357, 12 rue du Général Zimmer, 67084 Strasbourg, France.

Address correspondence to: Peter Rehling (peter.rehling{at}biochemie.uni-freiburg.de).




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