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J Gen Virol 44 (1979), 669-678; DOI 10.1099/0022-1317-44-3-669
© 1979 Society for General Microbiology
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In Vivo and In Vitro Phosphorylation of Murine Mammary Tumour Virus Proteins

Arnold S. Dion, Garland S. Fout and Anthony A. Pomenti

Department of Molecular Biology, Institute for Medical Research, Copewood Street, Camden, New Jersey 08103, U.S.A.

A comparative study of in vitro and in vivo phosphorylation of murine mammary tumour virus, a type B RNA virus, is reported. The protein kinase activity associated with murine mammary tumour virus catalysed the in vitro phosphorylation of endogenous virus polypeptides. This kinase activity required a divalent metal cation, a non-ionic detergent, and was stimulated in the presence of dithiothreitol. Exogenous cyclic AMP was not required. The 32P-labelled products of the in vitro reaction were completely sensitive to pronase digestion and the phosphate was attached mainly by phosphomonoester linkage to serine residues. As determined by SDS-polyacrylamide gel electrophoresis, heterogeneous labelling of major and minor virus polypeptides was observed under in vitro conditions.

In contrast, the in vivo labelling of type B virus produced by a continuous cell line (MuMT-73), established from pooled mammary adenocarcinomas of Balb/cfC3H mice, demonstrated specific phosphoproteins associated with murine mammary tumour virus. The major phosphorylated proteins were found to have mol. wt. of 18000 and 12000 (p18 and p12) after isolation by molecular sieving chromatography and analysis by gel electrophoresis.

Received 15 November 1978; accepted 22 February 1978.




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Copyright © 1979 by the Society for General Microbiology.