PMID:11943219

Citation	Arechaga, I, Butler, PJ and Walker, JE (2002) Self-assembly of ATP synthase subunit c rings. FEBS Lett. 515:189-93
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.
Links	PubMed
Keywords	Bacterial Proton-Translocating ATPases/chemistry; Bacterial Proton-Translocating ATPases/isolation & purification; Bacterial Proton-Translocating ATPases/ultrastructure; Detergents/chemistry; Dimethylamines/chemistry; Escherichia coli/chemistry; Escherichia coli/enzymology; Image Processing, Computer-Assisted; Microscopy, Electron; Molecular Weight; Protein Binding/physiology; Protein Subunits; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/ultrastructure; Ultracentrifugation/methods
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