Result: Foci of pATM were also detected in EBV-positive Raji cells expressing the
Table: R179A
Figure: (A) Raji cells infected with an empty vector lentivirus (V), or lentiviruses expressing the wild-type ZEBRA gene (A: i), Z(R179A) (A: ii), or Z(S186A) (A: iii) were fixed and double stained for ZEBRA and pATM.
Figure: ATM is phosphorylated upon expression of WT ZEBRA, and ZEBRA mutants Z(R179A), and Z(S186A) in Raji cells.
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.
Result: These foci of EA-D clumps produced in the presence of PAA and ACV were uneven in size, intensity, and spacing and did not resemble the uniformly sized
Figure: D98/HR-1 cells were transfected with wild-type ZEBRA (i-vi) or R179A mutant ZEBRA (vii-xviii).
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.
Abstract: Mutants competent to bind DNA could be separated into four functional groups: the wild-type group (eight mutants), a group defective at activating Rta (five mutants, all with mutations at the S186 site), a group defective at activating EA-D (three mutants with the R179A, S186T, and K192A mutations), and a group specifically defective at activating late gene expression (seven mutants).
EBV mutation literature information.
PMID: 
2015
PloS one
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