Wang, Jean Y. J. and Baltimore, David (1985) Localization of tyrosine kinase-coding region in v-abl oncogene by the expression of v-abl-encoded proteins in bacteria. Journal of Biological Chemistry, 260 (1). pp. 64-71. ISSN 0021-9258 http://resolver.caltech.edu/CaltechAUTHORS:WANjbc85
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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.
|Additional Information:||Copyright © 1985 by the American Society for Biochemistry and Molecular Biology. (Received for publication, July 23, 1984) This work was supported by the National Cancer Institute and a grant from the Camille and Henry Dreyfus Foundation to J.Y.J.W. and a National Science Foundation Grant PCM-8314300. Part of this work was completed while J.Y.J.W. was a postdoctoral fellow of the Jane Coffin Childs Memorial Fund for Medical Research. The costs of publication of this article were defrayed in part by the payment of page charge. This article must therefore be marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.|
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|Deposited On:||20 Sep 2007|
|Last Modified:||26 Dec 2012 09:43|
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