COOPERATIVE ASSEMBLY OF EBNA1 ON THE EPSTEIN-BARR-VIRUS LATENT ORIGINOF REPLICATION

The EBNA1 protein of Epstein-Barr virus (EBV) activates DNA replicatio n by binding to multiple copies of its 18-bp recognition sequence pres ent in the Epstein-Barr virus latent origin of DNA replication, oriP. Using electrophoretic mobility shift assays, we have localized the min imal DNA binding domain of EBNA1 to between amino acids 470 and 607. W e have also demonstrated that EBNA1 assembles cooperatively on the dya d symmetry subelement of oriP and that this cooperative interaction is mediated by residues within the minimal DNA binding and dimerization domain of EBNA1.