v-mos Protein produced by in vitro translation has protein kinase activity

N. K. Herzog, M. Nash, L. S. Ramagli, R. B. Arlinghaus

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

The v-mos protein, termed p37(v-mos), has a closely asociated serine/threonine protein kinase activity. To provide further information about its protein kinase activity, we tested the activity of p37(v-mos) produced in a cell-free translation system from transcripts generated from a cloned v-mos gene. Anti-mos(37-55) immuno-precipitates of in vitro-produced p37(v-mos) were found to posses serine/threonine protein kase activity, whereas those obtained with anti-mos(260-271), known to block v-mos autophosphorylation, lacked kinase activity. The phosphorylated products were identical in size to p37(v-mos) and p43(v-mos) produced in protein kinase assays from Moloney murine sarcoma virus-infected cells expressing authentic p37(v-mos). These results provide further proof that the protein kinase activity associated with p37(v-mos) is an intrinsic property of the v-mos gene product. This translation system also provides a useful-experimental model to study the activation of the mos protein kinase. Thus, protein kinase assays performed on [35S]methionine-labeled p37(v-mos) produced p43(v-mos) at the expense of p37(v-mos). Phosphatase treatment removed the p43(v-mos) species, resulting in an increase of the p37(v-mos)-sized protein, confirming our previous interpretation that p43(v-mos) is a hyperphosphorylated form of p37(v-mos)

Original languageEnglish (US)
Pages (from-to)3093-3096
Number of pages4
JournalJournal of virology
Volume64
Issue number6
DOIs
StatePublished - 1990

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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