Regulation of SV40 DNA replication by phosphorylation of T antigen.
The role of phosphorylation in regulating the biochemical properties of SV40 large T antigen has been examined. Treatment of purified T antigen with calf intestinal alkaline phosphatase resulted in the removal of 80% of the 32P label. This partially dephosphorylated T antigen displayed an increase in its ability to support DNA replication in vitro. This increase in replication activity was paralleled by an activation of specific DNA binding to site II, a necessary element within the origin of SV40 DNA replication. In contrast, the ATPase activity of dephosphorylated T antigen remained unchanged. These results demonstrate that DNA replication is regulated by phosphorylation of an origin specific DNA binding protein.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000378:metabolism*; D002460:Cell Line; D004261:DNA Replication; D004789:Enzyme Activation; D006367:HeLa Cells / Q000378:metabolism; D006706:Homeostasis; D006801:Humans; D007700:Kinetics; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013539:Simian virus 40 / Q000235:genetics*
D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D009856:Oncogene Proteins, Viral; D011494:Protein Kinases; D000469:Alkaline Phosphatase; D000251:Adenosine Triphosphatases