Abstract
DNA-dependent RNA polymerase was purified from uninfected and ϕ29-infected Bacillus amyloliquefaciens. Differences were observed in the specific activities, template specificities, stability, and sedimentation properties of the two enzymes. A polypeptide of 30,000 molecular weight was found in association with the polymerase of high specific activity from phage-infected cells and was absent from polymerase isolated from uninfected cells. The change in polymerase properties and the appearance of the polypeptide occurred early in phage infection.
Keywords: properties, subunit composition, time of modification
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