Phosphoprotein Component of Vaccinia Virions
AUTOR(ES)
Rosemond, Hortencia
RESUMO
The recent discovery of a protein kinase activity in vaccinia virions led us to search for a viral protein which is phosphorylated in vivo. Vaccinia virus was radioactively labeled by infecting cells in the presence of 32P1. A phosphoprotein was isolated from purified delipidated virions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The phosphoprotein appeared to be a specific viral component induced after infection. More than 60% of the phosphoprotein was associated with viral cores. The electrophoretic mobility of the protein suggested that it has a molecular weight of 11,000 to 12,000. Phosphoserine was liberated by acid hydrolysis and identified by electrophoresis with known standards. Tryptic digests of the purified phosphoprotein were analyzed by two-dimensional electrophoresis and chromatography on thin-layer cellulose plates, and a single major phosphopeptide was resolved. The high selectivity of phosphorylation suggested that the process has a specific function.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=355204Documentos Relacionados
- Vaccinia Virus Morphogenesis: A13 Phosphoprotein Is Required for Assembly of Mature Virions
- Investigation of Structural and Functional Motifs within the Vaccinia Virus A14 Phosphoprotein, an Essential Component of the Virion Membrane
- Early promoter-binding factor from vaccinia virions.
- Solubilization of a protein synthesis inhibitor from vaccinia virions.
- Phosphorylated protein component present in influenza virions.
