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. 1990 Sep;178(1):293-6.
doi: 10.1016/0042-6822(90)90407-i.

Interaction of Epstein-Barr viral (EBV) origin of replication (oriP) with EBNA-1 and cellular anti-EBNA-1 proteins

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Interaction of Epstein-Barr viral (EBV) origin of replication (oriP) with EBNA-1 and cellular anti-EBNA-1 proteins

L T Wen et al. Virology. 1990 Sep.

Abstract

We have previously shown that 12-O-tetradecanoylphorbol-13-acetate (TPA) which activates expression of the latent genome of the Epstein-Barr virus (EBV) in Burkitt lymphoma cells induces the synthesis of two cellular anti-EBNA-1 competitor proteins, anti-EBNA-1.1 and anti-EBNA-1.2. Both anti-EBNA-1 proteins can uncouple the specific binding of the EBNA-1 to the region required for EBV plasmid maintenance (oriP). Here, we show by DNase I footprinting that the binding sites on oriP for the EBNA-1 and the anti-EBNA-1 proteins were indistinguishable. The proteins bound to the 30-bp tandem repeats of the oriP. Glycerol-gradient centrifugation and gel retardation assay revealed that a 60-kDa protein formed the anti-EBNA-1.1-DNA complex and a 40-kDa protein formed the anti-EBNA-1.2-DNA complex.

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