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Published August 1980 | Published
Journal Article Open

A transformation-defective mutant of Abelson murine leukemia virus lacks protein kinase activity

Abstract

A transformation-defective mutant of Abelson murine leukemia virus (A-MuLV), called A-MuLV-P92td, has been isolated. The mutant encodes a serologically identifiable A-MuLV protein of molecular weight 92,000 (P92) but it lacks the ability to transform either fibroblasts or bone marrow lymphoid cells. In contrast to the protein made by transforming strains of A-MuLV, the protein made by A-MuLV-P92td does not becme phosphorylated during in vitro incubation with [γ-^(32)P]ATP. If the protein is mixed with proteins from cells transformed by a functional A-MuLV strain, phosphorylation of P92 occurs, showing that its ability to accept phosphate is not altered by the mutation. These parallel changes provide genetic evidence that the A-MuLV protein is a transforming protein and that its associated protein kinase activity (EC 2.7.1.37) is a crucial part of its transforming ability.

Additional Information

© 1980 National Academy of Sciences. Contributed by David Baltimore, April 21, 1980. This work was supported by U.S. Public Health Service Grant CA-24220 (to N.R.), Program Project Grant CA-24530 from the National Cancer Institute (to N.R.), Grant MV-34K from the American Cancer Society (to D.B.), and by U.S. Public Health Service Grant CA-14051 from the National Cancer Institute (Core Grant to S. E. Luria). O.N.W. was a Helen Hay Whitney Postdoctoral Fellow. N.R. is a recipient of a Research Scholar Award from the American Cancer Society (Massachusetts Division). D.B. is an American Cancer Society Research Professor. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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August 22, 2023
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