[Oligomeric assemblies of transport adenosine triphosphatases in a membrane bilayer].

The comparative analysis of the own and literature data concerning the oligomeric organization of membrane-bound transport ATPases is presented. The results show that functional activity of protomeres is distinct from that of oligomeric assembly. It was demonstrated that ATP regulated interprotomer interaction in the oligomers including their dissociation into individual protomers. Evidence for changeable amount of protomers interacting with each other at different stages of the hydrolytic cycle is presented. The hypothesis that membrane lipids regulate the activity of membrane-bound oligomeric proteins affecting the efficiency of interprotomer interactions within the oligomeric complexes is justified.