Isometric virus particles, 33 nm in diameter, were purified to apparent homogeneity from a dsRNA-containing isolate (Rhs 717) of anastomosis group 2 of the basidiomycete . The dsRNA segments isolated from purified particles had the same (1.5 × 10 and 1.4 × 10) as those isolated directly from mycelial tissue of Rhs 717. Purified virus particles had a buoyant density of 1.37 g/ml in CsCl, and an / ratio of 1.43. The melting curve of the mixture of dsRNA segments from Rhs 717 particles had a sharp thermal transition with a melting temperature of 95 °C in standard saline citrate buffer. The RNA polymerase activity associated with the purified virus was characterized. Enzyme activity was dependent on the presence of Mg and was insensitive to actinomycin D. Virus particles and RNA polymerase activity cosedimented as a single peak in isopycnic CsCl gradients. The major reaction products were two dsRNA segments of 1.5 × 10 and 1.4 × 10, which corresponded to those of the two viral dsRNAs. The [P]UMP-labelled products hybridized to the two viral dsRNAs. The RNA synthesized remained in association with virus particles subjected to agarose gel electrophoresis.


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