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J. Biol. Chem., Vol. 275, Issue 42, 32822-32831, October 20, 2000
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From the Laboratory of Fundamental Virology and Immunology,
Institute of Pathology B23, University of Liege,
B-4000 Liege, Belgium
Varicella-zoster virus (VZV) open reading frame
4-encoded protein (IE4) possesses transactivating properties for VZV
genes as well as for those of heterologous viruses. Since most
transcription factors act as dimers, IE4 dimerization was studied using
the mammalian two-hybrid system. Introduction of mutations in the IE4
open reading frame demonstrated that both the central region and the
carboxyl-terminal cysteine-rich domain were important for efficient
dimerization. Within the carboxyl-terminal domain, substitution of
amino acids encompassing residues 443-447 totally abolished
dimerization. Gene activation by IE4 was studied by transient
transfection with an IE4 expression plasmid and a reporter gene under
the control of either the human immunodeficiency virus, type 1, long
terminal repeat or the VZV thymidine kinase promoter. Regions of IE4
important for dimerization were also shown to be crucial for
transactivation. In addition, the arginine-rich domains Rb and Rc of
the amino-terminal region were also demonstrated to be important for
transactivation, whereas the Ra domain as well as an acidic and
bZIP-containing regions were shown to be dispensable for gene
transactivation. A nucleocytoplasmic shuttling of IE4 has also been
characterized, involving a nuclear localization signal identified
within the Rb domain and a nuclear export mechanism partially depending
on Crm-1.
Gene Activation by Varicella-Zoster Virus IE4 Protein Requires
Its Dimerization and Involves Both the Arginine-rich Sequence, the
Central Part, and the Carboxyl-terminal Cysteine-rich Region*
,
*
This work was supported in part by grants from the Belgian
National Fund for Scientific Research (Brussels, Belgium), the VZV
Research Foundation (New York), and the "Concerted Action Program"
(Communauté Française de Belgique, Brussels, Belgium).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a Belgian National Fund for Scientific Research
Scientific Collaborator grant.
§
Funded by the Belgian National Fund for Scientific Research and a
VZV Research Foundation Fellowship.
¶
Research Director at the Belgian National Fund for Scientific
Research. To whom correspondence should be addressed: Laboratory of
Fundamental Virology and Immunology, Institute of Pathology B23,
University of Liege, B-4000 Liege, Belgium. Tel.: 32-4-366-24-42; Fax:
32-4-366-24-33; E-mail: jpiette@ulg.ac.be.
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