About 30 per cent of cellular proteins are found in membranes. In eukaryotic cells, mitochondrial membrane proteins undergo a sequence of chaperoned transfers across a double- membrane system utilising dedicated mitochondrial translocases.

The targeting and transfer of membrane-spanning transporters through the intermembrane space requires specialised translocase components. Our structures of Tim9-Tim10 revealed a modular propeller-like fold, suggesting a previously unanticipated mode of chaperone activity and serving as a model for deriving function. Our objective is to experimentally define the interactions of mitochondrial carrier precursors with translocase components and to look at how translocase components co-assemble.