Answer
Cells of a Src alone is not oncogenic in nature they induce tumor as v-src. RNA, and antibody to v-src protein precipitates to form tumour cells that are clonal in nature. Karyotypic analysis shows that V-src oncogene alone is unable to induce cancer, the neoplastic transformation of SHE cells with which they bond and alter makes them oncogenic in nature.
a) The deletion or inactivation of the SH3 domain: Deletion of SH3 domain restores growth factor independence to P185 BCR ABL, MYC sequences are encoded by the ABL last exon, the SH3 and SH2 domains, v ABL sequences containing a myristoylation signal, co expressed MYC respectively. Deletion of SH3 domain hence restores autophosphorylation as well as transphosphotyrosine. Western blotting analysis of total cell lysates from Ba/F3 cells were infected. With a myristoylation signal SH3 domain deletion some the Ba/F3 cells that survived were also deprived of IL-3.
b) The mutation of Tyr 416 to Phe: In vitro autophosphorylation mutation strongly activated transformation and kinase activity during which Tyr was mutated to Phe 416 and also restricted stability of phosphorylation.
Work Step by Step
Cells of a Src alone is not oncogenic in nature they induce tumor as v-src. RNA, and antibody to v-src protein precipitates to form tumour cells that are clonal in nature. Karyotypic analysis shows that V-src oncogene alone is unable to induce cancer, the neoplastic transformation of SHE cells with which they bond and alter makes them oncogenic in nature.
a) The deletion or inactivation of the SH3 domain: Deletion of SH3 domain restores growth factor independence to P185 BCR ABL, MYC sequences are encoded by the ABL last exon, the SH3 and SH2 domains, v ABL sequences containing a myristoylation signal, co expressed MYC respectively. Deletion of SH3 domain hence restores autophosphorylation as well as transphosphotyrosine. Western blotting analysis of total cell lysates from Ba/F3 cells were infected. With a myristoylation signal SH3 domain deletion some the Ba/F3 cells that survived were also deprived of IL-3.
b) The mutation of Tyr 416 to Phe: In vitro autophosphorylation mutation strongly activated transformation and kinase activity during which Tyr was mutated to Phe 416 and also restricted stability of phosphorylation.
