Localization of tyrosine kinase-coding region in v-abl oncogene by the expression of v-abl-encoded proteins in bacteria.
A series of plasmids containing different segments of the v-abl oncogene have been constructed to express different portions of the v-abl protein in bacteria. The tyrosine kinase activity of these proteins was determined by an in vitro assay employing histones or angiotensin II as substrates for the v-abl-encoded tyrosine kinase. These experiments show that the 5'-1.2 kilobases of v-abl is necessary and sufficient to produce an active tyrosine kinase which is functional as a monomeric soluble protein. The kinase-coding region corresponds to the minimal region of v-abl required for the transformation of fibroblasts. The kinase-coding region also coincides with the conserved protein sequences which are found in other tyrosine kinases. A compact domain of the v-abl protein including this kinase-coding region can accumulate to high levels in bacteria. The C-terminal region of the v-abl protein is not needed for the kinase activity and is rapidly degraded in bacteria.
Wang
J Y
JY
Baltimore
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D000011:Abelson murine leukemia virus / Q000235:genetics*; D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D009052:Leukemia Virus, Murine / Q000235:genetics*; D051379:Mice; D008970:Molecular Weight; D009857:Oncogenes; D010766:Phosphorylation; D010957:Plasmids; D006656:Protamine Kinase / Q000235:genetics; D011494:Protein Kinases / Q000235:genetics*; D011505:Protein-Tyrosine Kinases
D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D006656:Protamine Kinase