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Updated: Aug 8, 2026

Temporal Quantification of MAPK Induced Expression in Single Yeast Cells
Published on: October 4, 2013
Moloney murine sarcoma virus encoded p37mos expressed in yeast has protein kinase activity
Abstract:
We describe the expression of the Moloney murine sarcoma virus env-mos protein (p37mos) in yeast under the control of the yeast GAL1 promoter. Consistent with our previous results concerning the p37mos protein kinase made in virus infected mouse cells, p37mos produced in yeast possesses autophosphorylation activity in an immune complex kinase assay using anti-mos (37-35) serum.
Insights
The Moloney murine sarcoma virus env-mos protein (p37mos) was successfully expressed in yeast. The yeast-produced p37mos protein kinase demonstrated autophosphorylation activity, consistent with findings in mouse cells.
Area of Science:
- Molecular Biology
- Virology
- Yeast Genetics
Background:
- The Moloney murine sarcoma virus env-mos protein (p37mos) is a known protein kinase.
- Previous studies characterized p37mos activity in virus-infected mouse cells.
Purpose of the Study:
- To express the Moloney murine sarcoma virus env-mos protein (p37mos) in yeast.
- To characterize the biochemical activity of yeast-produced p37mos.
Main Methods:
- Gene expression in yeast using the GAL1 promoter.
- Immune complex kinase assay using anti-mos (37-35) serum.
Main Results:
- Successful expression of p37mos in yeast.
- Yeast-produced p37mos exhibited autophosphorylation activity.
- Activity of yeast-derived p37mos was consistent with that from mouse cells.
Conclusions:
- Yeast is a viable system for producing functional p37mos protein.
- The autophosphorylation activity of p37mos is conserved in yeast expression systems.
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