Self-assembly of ATP synthase subunit c rings.
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.
Arechaga
Ignacio
I
The Medical Research Council Dunn Human Nutrition Unit, Hills Road, CB2 2YK, Cambridge, UK.
Butler
P Jonathan G
PJ
Walker
John E
JE
D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D003902:Detergents / Q000737:chemistry; D004123:Dimethylamines / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology*; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D008970:Molecular Weight; D011485:Protein Binding / Q000502:physiology; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure; D014461:Ultracentrifugation / Q000379:methods
D003902:Detergents; D004123:Dimethylamines; D021122:Protein Subunits; D011994:Recombinant Proteins; C014518:dodecyldimethylamine oxide; D025243:Bacterial Proton-Translocating ATPases