Important note: Information in this article was accurate in 1990. The state of the art may have changed since the publication date.
EXPRESSION AND FUNCTIONAL DOMAINS OF THE TRANSFORMING PROTEIN OF AVIAN SARCOMA VIRUS UR2
Diss Abstr Int [B]; 51(1):77 1990. Unique Identifier : AIDSLINE ICDB/90667067 Jong SJ; Rockefeller Univ.
Abstract:
In order to study the mechanisms of cell transformation by the avian sarcoma virus UR2 which contains the oncogene ros, antibodies against its product P68gag-ros were developed. They were raised against ros-specific oligo- and poly-peptides. The antibodies were used to monitor the expression of potential c-ros product and detected a p110 in human glioblastoma cell lines U138 and U343. Site-directed mutagenesis of the P68 coding sequence with recombinant DNA techniques was used to dissect the functional domains of P68. It was found that the gag sequence, the hydrophobic domain, and the kinase domain are all important for cell transformation. The localization and potential substrates of the P68 kinase were also examined. P68 was found to span the plasma membrane with the p19(gag) portion protruding extracellularly. The potential substrates of P68, a transmembrane tyrosine protein kinase, were found to be less complicated than those found for non-transmembrane tyrosine protein kinases such as pp60src, a property apparently shared by other receptor kinases such as the insulin receptor. A recombinant between the two oncogenes, src and ros, was constructed, called SRC-ROS, with the N-terminus from src and the kinase domain from ros. The protein product of the SRC-ROS is likely to be associated with cell membranes in a way similar to the src gene product of Rous sarcoma virus (RSV) because it contains the 5' src sequence, is myristylated, and lacks a transmembrane domain. The SRC-ROS transformed chicken embryo fibroblasts into a fusiform morphology, similar to that by UR2. When the substrates for the SRC-ROS were examined, they showed similarity to RSV(src) rather than UR2(ros). The substrate specificity, therefore, appeared to be correlated with the localization of the transforming protein, but not with the catalytic domains of the kinases. (Full text available from University Microfilms International, Ann Arbor, MI, as Order No. AAD90-16121)
Keywords: Animal Cell Transformation, Viral/*GENETICS Chick Embryo *Gene Expression Regulation, Viral Gene Products, gag/*GENETICS *Genes, gag Glioma/GENETICS Human Protein-Tyrosine Kinase/GENETICS Recombination, Genetic Sarcoma Viruses, Avian/*GENETICS Substrate Specificity Tumor Cells, Cultured THESIS 901230
M90C3723
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Important note: Information in this article was accurate in 1990. The state of the art may have changed since the publication date.
