Replacing C189 in the bZIP domain of Zta with S, T, V, or A changes DNA binding specificity to four types of double-stranded DNA.
PMID: 29772230
2018
Biochemical and biophysical research communications
Result: Zta(C189S) and Zta(C189T), and Zta(C189A) and Zta(C189V) bind DNA(C C) 8-mers similarly, as may be expected as these pairs of amino acids have similar physico-chemical properties (Fig S3A-B).
Result: Zta(C189S) binds several 8-mers containing the hydroxymethylated C/EBP half-site GH2AA, sim
Discussion: Zta(C189S) and Zta(C189T) bound the TRE motif (TGAG/CTCA) stronger than Zta while binding to all other sequences was reduced.
Methylation-dependent binding of the epstein-barr virus BZLF1 protein to viral promoters.
Result: To determine whether Z residue 186 or 189 regulates Z binding to methylated ZREs in Nap, we compared the ability of in vitro-translated wild-type Z, Z(S186A) and Z(C189S) to bind to labeled oligonucleotide probes containing the Nap ZRE1 and ZRE2 sites, the consensus AP1 site from the BMRF1 early viral promoter, or the Rp ZRE2 and ZRE3 sites.
Figure: Wild-type Z (WTZ), Z(S186A), Z(C189S) or empty vector (vector) were transfected in to 293 Z-KO cells in the presence
Epstein-Barr virus immediate-early protein Zta co-opts mitochondrial single-stranded DNA binding protein to promote viral and inhibit mitochondrial DNA replication.
Abstract: A point mutation in the Zta DNA binding domain (C189S), which is known to reduce lytic cycle replication, eliminated mtSSB association with Zta.
Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein.
Discussion: In particular, the model rationalizes why the binding affinity of Zta for unmethylated ZRE3 is lower than for ZRE2, why methylation increases the binding affinity for both sites, why the C189S mutation compromises methyl-ZRE recognition, and why the latter effect is more pronounced for ZRE3 than for ZRE2.
Discussion: More specifically, because ZtaC189S is severely compromised for meZRE3 (but not meZRE2) binding, the inability of this mutant to activate BRLF1 expression in Raji cells suggests that meZRE3 recognition is particularly critical for Rp activation in this cell line (Figure 1).
Discussion: Thus, the C189S mutant provides a highly selective tool to address the relevance of methylated ZRE recognition for the disruption of latency in vivo.
The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein.
PMID: 18631132
2008
Biochemical Society transactions
Abstract: ZtaC189S was not able to activate Rp in a B-cell line, demonstrating the relevance of the interaction with methylated ZREs.
Abstract: A single point mutant of Zta, C189S, is defective in binding to the methylated ZREs both in vitro and in vivo.
A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication.
Abstract: C189S was deficient for transcription activation of several viral late genes that depend on lytic replication and therefore was consistent with a primary defect of C189S in activating lytic replication.
Abstract: C189S was not defective in binding methylated DNA binding sites and was capable of activating Rta from endogenous latent viral genomes, in contrast to the previously characterized S186A mutation.
Abstract: C189S was slightly impaired for its ability to form a stable complex with Rta, although this did not prevent Rta recruitment to OriLyt.
Abstract: In this work, we show that replacement of C189 with serine (C189S) eliminated lytic
EBV mutation literature information.
PMID: 
2018
Biochemical and biophysical research communications
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