NCP98 and its associated kinase activity are found predominantly (60-90%) in the soluble fraction of chicken myeloblasts, unlike its viral homolog P140 which is predominantly particulate.
Association with cellular structural components correlates with the transforming activity of proteins containing fps sequences.
We compared the intracellular location of the product of the c-fps proto-oncogene, NCP98, with that of its viral homolog P140, the transforming protein of Fujinami sarcoma virus. Using the technique of biochemical subcellular fractionation, we determined that 60 to 90% of NCP98 and its associated kinase activity are in the soluble fraction of a chicken myeloblast cell line. This fractionation behavior differs from that of P140, which is found predominantly in the particulate fraction, both in Fujinami sarcoma virus-infected chicken embryo fibroblasts and in Fujinami sarcoma virus-infected myeloblasts. The fractionation behavior of NCP98 is, however, similar to that of the P140 encoded by a temperature-sensitive strain of Fujinami sarcoma virus in infected cells grown at the nonpermissive temperature. The absence of gag sequences from NCP98 is not responsible for the difference in fractionation behavior: the v-fps transforming protein of strain F36, P91, which lacks gag sequences, is also predominantly particulate. These results indicate that association with cellular structural components correlates with the transforming activity of proteins containing fps sequences.
Young et al. (Sat,) reported a other. NCP98 vs. P140 was evaluated on Intracellular location (soluble vs particulate fraction). NCP98 and its associated kinase activity are found predominantly (60-90%) in the soluble fraction of chicken myeloblasts, unlike its viral homolog P140 which is predominantly particulate.