|Title||Self-assembly of ATP synthase subunit c rings.|
|Publication Type||Journal Article|
|Year of Publication||2002|
|Authors||Arechaga, I, P Butler, JG, Walker, JE|
|Date Published||2002 Mar 27|
|Keywords||Bacterial Proton-Translocating ATPases, Detergents, Dimethylamines, Escherichia coli, Image Processing, Computer-Assisted, Microscopy, Electron, Molecular Weight, Protein Binding, Protein Subunits, Recombinant Proteins, Ultracentrifugation|
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.
|Alternate Journal||FEBS Lett.|