Mohr I J, Stillman B, Gluzman Y
EMBO J. 1987 Jan;6(1):153-60. doi: 10.1002/j.1460-2075.1987.tb04733.x.
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.
磷酸化在调节SV40大T抗原生化特性中的作用已得到研究。用小牛肠碱性磷酸酶处理纯化的T抗原，导致80%的32P标记被去除。这种部分去磷酸化的T抗原在体外支持DNA复制的能力有所增加。复制活性的这种增加与对位点II的特异性DNA结合的激活相平行，位点II是SV40 DNA复制起点内的一个必要元件。相反，去磷酸化T抗原的ATP酶活性保持不变。这些结果表明，DNA复制受一种起点特异性DNA结合蛋白的磷酸化调节。
