Purification of a ribonucleic acid-dependent ribonucleic acid polymerase from leukemic cells Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/m900nx356

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  • There is good evidence that the infection with avian myeloblastosis virus BAI strain A causes myeloblasts to retain their primitive nature. These cells are able to multiply and produce virus at a relatively constant rate. From these observations, a major problem develops in the study of the virus-induced leukemia, that of the mechanism for replication of the viral RNA genome. Consideration was given to the enzyme(s) involved in viral RNA synthesis. Evidence was given for the presence of a RNA polymerase absolutely dependent upon the presence of exogenous RNA template for enzyme activity. DNA-dependent RNA polymerase and a poly A-dependent poly A polymerase were removed by the fractionation procedure. Polyvinyl sulfate, a known inactivator of ribonuclease, was used to inhibit a ribonuclease activity associated with the RNA-dependent RNA polymerase. In the presence of polyvinyl sulfate, the polymerase evidenced a specificity for high molecular weight viral RNA as template for synthesis of RNA product sedimenting with preserved RNA template as determined by glycerol gradient centrifugation. There was also shown an absolute requirement for all four ribonucleoside triphosphates by the enzyme in the presence of polyvinyl sulfate and high molecular weight viral RNA. The reaction product, using high molecular weight viral RNA as template, was analyzed for sedimentation rate as compared to the template RNA. It was found to sediment with the high molecular weight viral RNA template. Nearest neighbor analysis of the product indicates synthesis of a RNA heteropolymer. There is tenous evidence for a complementary copying mechanism being utilized for synthesis of the RNA product, since the product is easily dissociable from the template. Annealing the dissociated product with RNA template results in small amounts of ribonuclease-resistance. The RNA-dependent RNA polymerase can be dissociated into at least two components which maintain an enzyme activity dependent upon exogenous RNA. These separated components are distinguished by the ribonucleoside triphosphates they utilize. Neither component has been shown to be capable of synthesizing high molecular weight RNA product with the high molecular weight viral RNA as template. Nearest neighbor frequencies of the RNA product are very different. A complex of the RNA polymerase and associated RNA has been examined with less detail.
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