Abstract
Many viral oncogenes encode protein~yrosine kinase activities. However, importantin vivo substrates of these enzymes have yet to be identified. Recently, type I topoisomerases were shown to bein vitro substrates for two tyrosine kinases. Following tyrosine phosphorylation, topoisomerase I activity was reduced 10-fold (Tse-Dinhet al. Nature 312:785–786, 1984). To determine whether topoisomerase I activity was modulated by tyrosine phosphorylationin vivo, we have measured topoisomerase I activity in nuclear lysates prepared from both normal fibroblasts and cells transformed by two different viral oncogenes (v-abl, v-src). Under a variety of experimental conditions, we have found no evidence to support the notion that type I topoisomerase activity is modulated by tyrosine phosphorylationin vivo.
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Colledge, W.H., Edge, M. & Foulkes, J.G. A comparison of topoisomerase I activity in normal and transformed cells. Biosci Rep 6, 301–307 (1986). https://doi.org/10.1007/BF01115159
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DOI: https://doi.org/10.1007/BF01115159