Oc. Richards et E. Ehrenfeld, EFFECTS OF POLIOVIRUS 3AB PROTEIN ON 3D POLYMERASE-CATALYZED REACTION, The Journal of biological chemistry, 273(21), 1998, pp. 12832-12840
Poliovirus RNA replication requires the activities of a viral RNA-depe
ndent RNA polymerase, 3D(pol), in conjunction with several additional
viral and likely cellular proteins. The importance of both the 3A and
3B coding regions has been documented previously by genetic tests, and
their biochemical activities have been the subject of several recent
investigations. In this study, we examined the previously reported sti
mulation of 3D-catalyzed RNA synthesis by 3AB, We show that 3AB does n
ot stimulate RNA synthesis on templates that are stably base paired to
a primer, indicating that 3AB does not stabilize or otherwise activat
e 3D(pol) for chain elongation. Similarly, it does not alter the kinet
ic parameters or binding affinities of 3D for substrates. In the absen
ce of a primer, or in the presence of a primer that does not form a st
able hybrid with the template, 3AB increases the utilization of 3'-hyd
roxyl termini as sites for chain elongation by 3D, and thereby stimula
tes RNA synthesis, 3AB may interact with and stabilize these sites and
/or may recruit 3D(pol) to the site, resulting in stimulation of the i
nitiation of elongation events. We propose that this activity is requi
red for stabilizing weak interactions that occur during nucleotidyl-pr
otein-primed initiation events in the viral RNA replication complex.