Escherichia coil Rho factor is required for termination of transcripti
on at certain sites by RNA polymerase. Binding to unstructured cytosin
e-containing RNA target sites, subsequent RNA-dependent ATP hydrolysis
, and an RNA-DNA helicase activity that presumably facilitates termina
tion, are considered essential for Rho function. Yet the RNA recogniti
on elements have remained elusive, the parameters relating RNA binding
to ATPase activation have been obscure, and the mechanistic steps tha
t integrate Rho's characteristics with its termination function in vit
ro and in vivo have been largely undefined. Recent work offers new ins
ights into these interactions with results that are both surprising an
d satisfying in the context of Rho's emerging structure. These include
the requirements for binding and ATPase activation by a variety of RN
A substrates, dynamic analyses of Rho tracking, helicase and terminati
on activity, and the participation of a new factor (NusG) that interac
ts with Rho. Models for Rho function are considered in the light of th
ese recent revelations.