Reference : Gene activation by varicella-zoster virus IE4 protein requires its dimerization and invo...
Scientific journals : Article
Human health sciences : Immunology & infectious disease
http://hdl.handle.net/2268/5175
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
English
Baudoux, Laurence [> > > >]
Defechereux, Patricia [> > > >]
Rentier, Bernard mailto [Université de Liège - ULg > Département de Microbiologie > Virologie fondamentale et Immunologie > >]
Piette, Jacques mailto [Université de Liège - ULg > Département des sciences de la vie > Virologie - Immunologie >]
20-Oct-2000
Journal of Biological Chemistry
American Society of Biochemistry and Molecular Biology
275
42
32822-32831
Yes (verified by ORBi)
International
0021-9258
[en] Varicella-Zoster virus ; Viral Latency ; Viral replication control
[en] 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 Re 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.
Researchers
http://hdl.handle.net/2268/5175
10.1074/jbc.M001444200
http://www.jbc.org/misc/Copyright_Permission.shtml

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