A quaternary transcription termination complex. Reciprocal stabilization by Rho factor and NusG protein.

The Escherichia coli protein NusG is known to modulate Rho-dependent transcription termination in vivo. We have shown that it can also alter the pattern of Rho-dependent RNA endpoints in vitro, at lower NusG concentrations than can be explained by reported interactions between NusG and Rho or RNA polymerase. Three observations in vitro now suggest a model to account for these effects of NusG on Rho-dependent termination. First, the presence of NusG circumvents the interference with Rho function caused by adding DNA oligonucleotides complementary to particular segments of the Rho binding site. Second, when NusG is added to stalled elongation complexes, the off-rate of Rho from nascent RNA is slowed. Third, NusG associates stably with the elongation complex only when Rho is also present and bound to the nascent RNA. Our observations are consistent with a model in which NusG and Rho participate in an interdependent association with the transcribing RNA polymerase and the nascent RNA to facilitate the recognition and use of termination signals. Common structural and functional features shared with complexes that carry out processive antitermination are discussed.