Self-assembly of ATP synthase subunit c rings.

Abstract

Subunit c of the H(+) transporting ATP synthase is an essential part of its membrane domain that participates in transmembrane proton conduction. The annular architecture of the subunit c from different species has been previously reported. However, little is known about the type of interactions that affect the formation of c-rings in the ATPase complex. Here we report that subunit c over-expressed in Escherichia coli and purified in non-ionic detergent solutions self-assembles into annular structures in the absence of other subunits of the complex. The results suggest that the ability of subunit c to form rings is determined by its primary structure.

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@article{Arechaga2002SelfassemblyOA, title={Self-assembly of ATP synthase subunit c rings.}, author={Ignacio Arechaga and P. Jonathan G. Butler and John E Walker}, journal={FEBS letters}, year={2002}, volume={515 1-3}, pages={189-93} }