Free RNA-dependent ATPase activity of transcription termination factor Rho: a model of cyclic dissociation and reassembly of Rho protein

RNA-dependent ATPase activity of Rho + and two mutant proteins Rho15 and Rho301 was studied. It was shown that monomeric Rho forms oligomers in the presence of ATP. This ATP-induced structural change of Rho allows protection of the protein from heat inactivation. Poly(C), which highly activates Rho ATPase, was found to potentiate heat inactivation of Rho301, but no Rho + and Rho15, only under optimal conditions of ATP hydrolysis. It was also shown that Rho301 is defective in interaction with RNA. The molecular model postulating that Rho-catalysed ATP hydrolysis with free RNA involves the cyclic process of protein dissociation and reassembly is postulated.