Abstract
Purified vaccinia virus treated with Triton X-100 catalyzes the incorporation of ATP into an acid-insoluble product. The enzymatic activity responsible for the ATP polymerization is demonstrated to be different from vaccinia RNA polymerase in its preferential use of ATP as substrate and on the basis of heat stability, pH optima, and metal ion requirement. The ATP polymerization reaction is stimulated 10-fold by the addition of rA(pA)5. In accordance with our earlier terminology, we call this Mn2+-dependent enzyme terminal riboadenylate transferase to distinguish it from Mg2+-dependent poly A polymerase.
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