Abstract
The v-mos protein, termed p37v-mos, has a closely associated serine/threonine protein kinase activity. To provide further information about its protein kinase activity, we tested the activity of p37v-mos produced in a cell-free translation system from transcripts generated from a cloned v-mos gene. Anti-mos(37-55) immunoprecipitates of in vitro-produced p37v-mos were found to possess serine/threonine protein kinase 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 p37v-mos and p43v-mos produced in protein kinase assays from Moloney murine sarcoma virus-infected cells expressing authentic p37v-mos. These results provide further proof that the protein kinase activity associated with p37v-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 p37v-mos produced p43v-mos at the expense of p37v-mos. Phosphatase treatment removed the p43v-mos species, resulting in increase of the p37v-mos-sized protein, confirming our previous interpretation that p43v-mos is a hyperphosphorylated form of p37v-mos.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.