Self-assembly of ATP synthase subunit c rings.

TitleSelf-assembly of ATP synthase subunit c rings.
Publication TypeJournal Article
Year of Publication2002
AuthorsArechaga, I, P Butler, JG, Walker, JE
JournalFEBS Lett
Date Published2002 Mar 27
KeywordsBacterial 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 JournalFEBS Lett.
Citation Key10.1016/s0014-5793(02)02447-x
PubMed ID11943219