Cardiolipin interaction with subunit c of ATP synthase: Solid-state NMR characterization

• Cardiolipin, a chemically unusual lipid, copurifies with subunit c of ATP synthase.
• Furthermore, NMR data indicate that cardiolipin interacts with cardiolipin.
• Association occurs both for subunit c of E. coli and S. pneumoniae.
• These studies suggest that F0 has specific interactions with cardiolipin.

The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces. Guest Editors: Lynette Cegelski and David P. Weliky.

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