Regulation of SV40 DNA replication by phosphorylation of T antigen.
AUTOR(ES)
Mohr, I J
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=553371Documentos Relacionados
- Mechanisms of interference with simian virus 40 (SV40) DNA replication by trans-dominant mutants of SV40 large T antigen.
- Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication.
- Interaction of DNA polymerase alpha-primase with cellular replication protein A and SV40 T antigen.
- c-myc protein can be substituted for SV40 T antigen in SV40 DNA replication.
- Simian virus 40 (SV40) small t antigen inhibits SV40 DNA replication in vitro.
