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Localization of the Abelson murine leukemia virus protein in a detergent-insoluble subcellular matrix: architecture of the protein

Boss, Michael A. and Dreyfuss, Gideon and Baltimore, David (1981) Localization of the Abelson murine leukemia virus protein in a detergent-insoluble subcellular matrix: architecture of the protein. Journal of Virology, 40 (2). pp. 472-481. ISSN 0022-538X.

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We examined the interaction of Abelson murine leukemia virus protein P120 with other cellular components after extraction with the nonionic detergent Triton X-100. Most of the Abelson murine leukemia virus P120-associated kinase activity was found in the detergent-insoluble matrix in both lymphoid and fibroblast cell lines. The P120 labeled during a short exposure of cells to [35S]-methionine was mainly in the detergent-insoluble matrix (lymphoid cells) or equally distributed in the detergent-insoluble matrix and the soluble fraction (fibroblasts). Steady-state-labeled P120 was distributed equally in the two fractions (lymphoid cells) or mostly in the soluble portion (fibroblasts). Thus, there was an apparent movement of P120 from the detergent-insoluble matrix to the detergent-soluble fraction and a concomitant loss of enzymatic activity. When the detergent-insoluble matrix was incubated with [32P]ATP in situ, phosphorylation of tyrosine residues of P120 was observed. We found an 80,000-molecular-weight fragment of P120 (designated F80) after extraction of fibroblast cells with detergent. F80 was not found in extracted lymphoid cells, but mixing labeled lymphoid cells and unlabeled fibroblasts before extraction produced the fragment. F80 contained the gag determinants of P120 but did not react with Abelson-specific serum. These data allowed us to assign various features of the protein to regions of the P120 molecule and to localize the Abelson-specific antigenic determinants to the C-terminal region of the molecule.

Item Type:Article
Baltimore, David0000-0001-8723-8190
Additional Information:Copyright © 1981 by the American Society for Microbiology. Received 21 April 1981/Accepted 24 June 1981. This work was supported by grant MV-34L from the American Cancer Society and by Public Health Service grant CA-14051 from the National Cancer Institute (core grant to S.E. Luria). M.A.B. is a postdoctoral fellow of the Science Research Council. G.D. is a postdoctoral fellow of the Helen Hay Whitney Foundation. D.B. is a Research Professor of the American Cancer Society.
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Record Number:CaltechAUTHORS:BOSjvir81
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ID Code:10960
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Deposited On:21 Jun 2008
Last Modified:31 Oct 2017 18:06

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