Result: We found that co-expression of the six core components of the replication machinery enhanced binding of wt ZEBRA, Z(Y180E), Z(R187K) and Z(S173A) to oriLyt by 2.1-, 6.0-, 16.4- and 5.0-fold, respectively.
Result: We found that over-expression of BBLF2/3 had no effect on the level of the late protein, FR3, induced by wt ZEBRA, Z(S173A) or Z(Y180E).
Mutations of amino acids in the DNA-recognition domain of Epstein-Barr virus ZEBRA protein alter its sub-nuclear localization and affect formation of replication compartments.
Result: The non-uniform and uneven distribution of R179A and Y180E proteins observed in 293 cells could be clearly distinguished from the pattern of distinctly-defined and evenly spaced discrete punctate foci seen in 2089 and BZKO cells containing EBV-bacmids.
Result: The speckled distribution of ZEBRA mutants, such as R179A and Y180E, in 293 cells containing EBV-bacmids is a new phenomenon.
Discussion: It should also be noted, however, that the roughly textured distribution pattern of the R179A and Y180E mutants in 293 cells differed from the smooth, even distribution seen with wild-type ZEBRA in the same cell type.
Amino acids in the basic domain of Epstein-Barr virus ZEBRA protein play distinct roles in DNA binding, activation of early lytic gene expression, and promotion of viral DNA replication.
EBV mutation literature information.
PMID: 
2010
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