Chemical modification of DNA polymerase phosphoprotein from avian myeloblastosis virus.
Fractionation of purified avian myeloblastosis virus DNA polymerase, after phosphorylation in vitro, revealed the presence of a small acidic proten, a phosphate acceptor polypeptide with high specific activity. Its presence in the phosphorylated form with the polymerase resulted in as much as a 10-fold increase in the rate of DNA synthesis. Its presence in the dephosphorylated form with the polymerase had no effect in the rate of DNA synthesis.
D001354:Avian Leukosis Virus / Q000201:enzymology*; D009189:Avian Myeloblastosis Virus / Q000201:enzymology* / Q000254:growth & development; D008956:Models, Chemical; D010750:Phosphoproteins / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000032:analysis*; D013329:Structure-Activity Relationship; D014779:Virus Replication
D010750:Phosphoproteins; D011494:Protein Kinases; D012194:RNA-Directed DNA Polymerase; D010744:Phosphoric Monoester Hydrolases