Tafazzin is a transacylase that affects cardiolipin fatty acid composition and 
mitochondrial function. Mutations in human tafazzin cause Barth syndrome yet the 
enzyme has mostly been characterized in yeast. To study tafazzin in higher 
organisms, we isolated mitochondria from Drosophila and mammalian cell cultures. 
Our data indicate that tafazzin binds to multiple protein complexes in these 
organisms, and that the interactions of tafazzin lack strong specificity. Very 
large tafazzin complexes could only be detected in the presence of cardiolipin, 
but smaller complexes remained intact even upon treatment with phospholipase A2. 
In mammalian cells, tafazzin had a half-life of only 3-6h, which was much 
shorter than the half-life of other mitochondrial proteins. The data suggest 
that tafazzin is a transient resident of multiple protein complexes.