Polynucleotide synthetase of E. coli: An enzyme complex having polynucleotide phosphorylase as apoenzyme

Abstract

A previously described synthetase system of Escherichia coli that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter — an enzyme incorporating nucleoside diphosphates — is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.