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 language | English (US) |
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Pages (from-to) | 3093-3096 |
Number of pages | 4 |
Journal | Journal of virology |
Volume | 64 |
Issue number | 6 |
DOIs | |
State | Published - 1990 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology