Summers H, Barwell J A, Pfuetzner R A, Edwards A M, Frappier L
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
J Virol. 1996 Feb;70(2):1228-31. doi: 10.1128/JVI.70.2.1228-1231.1996.
The EBNA1 protein of Epstein-Barr virus (EBV) activates DNA replication by binding to multiple copies of its 18-bp recognition sequence present in the Epstein-Barr virus latent origin of DNA replication, oriP. Using electrophoretic mobility shift assays, we have localized the minimal DNA binding domain of EBNA1 to between amino acids 470 and 607. We have also demonstrated that EBNA1 assembles cooperatively on the dyad symmetry subelement of oriP and that this cooperative interaction is mediated by residues within the minimal DNA binding and dimerization domain of EBNA1.
爱泼斯坦-巴尔病毒（EBV）的EBNA1蛋白通过结合存在于爱泼斯坦-巴尔病毒DNA复制潜伏起点oriP中的多个18碱基对识别序列拷贝来激活DNA复制。通过电泳迁移率变动分析，我们已将EBNA1的最小DNA结合结构域定位在氨基酸470至607之间。我们还证明EBNA1在oriP的二元对称亚元件上协同组装，并且这种协同相互作用由EBNA1最小DNA结合和二聚化结构域内的残基介导。
