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Serine- and threonine-specific protein kinase activities of purified gag–mil and gag–raf proteins

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Abstract

Retroviruses carry cell-derived oncogenes (v-onc) that have the potential to transform cells in culture and induce tumours in vivo1,2. One of the few carcinoma-inducing viruses is the acutely transforming retrovirus MH2 (refs 2,3), which carries the putative oncogene v-mil and the known oncogene v-myc(refs 4–6). Recently, a high degree of homology was discovered between v-mil and v-raf (ref. 7), the transforming gene of the murine retrovirus 3611 murine sarcoma virus (MSV)8, whereas homology to v-src is low9. Both viruses express their oncogenes as the gag-fusion polyproteins6,10 p100gag-mil and p75gag-raf (of respective relative molecular mass (Mr) 100,000 and 75,000), while the myc oncogene of MH2 is expressed by means of a subgenomic messenger RNA11. We have recently demonstrated that p100gag-mil is not a nuclear protein6. Here we report that purified p100gag-mil and p75gag-raf exhibit protein kinase activities in vitro which, in contrast to the src-related p130gag-fps of Fujinami sarcoma virus (FSV)12 and all other characterized oncogene-encoded protein kinases, phosphorylate serine and threonine but not tyrosine. Both types of protein kinases phosphorylate lipids in vitro.

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Authors and Affiliations

  1. Max-Planck-Institut für Molekulare Genetik, Abt. Schuster, Ihnestrasse 63, D-1000, Berlin (West), 33, FRG

    Karin Moelling, Barbara Heimann, Peter Beimling & Thomas Sander

  2. Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick Cancer Research Facility, Frederick, Maryland, 21701, USA

    Ulf R. Rapp

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  1. Karin Moelling
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  2. Barbara Heimann
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  3. Peter Beimling
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  4. Ulf R. Rapp
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  5. Thomas Sander
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Moelling, K., Heimann, B., Beimling, P. et al. Serine- and threonine-specific protein kinase activities of purified gag–mil and gag–raf proteins. Nature 312, 558–561 (1984). https://doi.org/10.1038/312558a0

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