ATP synthase: Subunit-subunit interactions in the stator stalk

In ATP synthase, proton translocation through the F-o subcomplex and ATP synthesis/hydrolysis in the F-1 subcomplex are coupled by subunit rotation. The static, non-rotating portions of F-1 and F-o are attached to each other via the peripheral "stator stalk", which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b(2)delta; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit delta (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F-1. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review. (c) 2006 Elsevier B.V. All rights reserved.