The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif.

@article{Chang1990TheEV,
  title={The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif.},
  author={Y N Chang and Ding-gui Dong and Gary S. Hayward and Stephen D. Hayward},
  journal={Journal of virology},
  year={1990},
  volume={64 7},
  pages={3358-69}
}
Introduction of the zta gene of Epstein-Barr virus into latently infected B cells leads to induction of the entire lytic cycle program of the virus. The Zta gene product is a sequence-specific DNA-binding protein of 35 kilodaltons that behaves as a specific transcriptional transactivator in transient cotransfection assays. All known Zta-responsive target promoters contain one or more members of a family of consensus-binding sites known as ZREs. On the basis of the presence of limited amino acid… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 54 extracted citations

Similar Papers

Loading similar papers…