ATP Phosphohydrolase (ATPase) Activity of a Polyoma Virus T Antigen

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Abstract
Among the various polyoma virus T antigens which were so far identified, only the large-T and a 63,000-MW polypeptide were bound to double-stranded calf thymus DNA. The proteins were not retained on single-stranded DNA-cellulose columns, and a purification procedure was designed on the basis of this observation. Purified fractions (approximately 1000-fold) exhibited an enzymatic activity which converts ATP into ADP and Pi. This activity was quantitatively inhibited after preincubation in the presence of anti-(polyoma T antigen) immunoglobulins and was dependent on a virus-coded gene product (a gene) on the basis of the following observations: ATPase activity from [mouse fibroblast 3T6 cells] infected with tsa mutants of polyoma was reduced after a shift to the restrictive temperature; the enzyme purified from tsa-infected cells maintained at the permissive temperature was more thermolabile in vitro than that prepared in parallel from cells infected with wild-type virus.