The equine herpesvirus 1 EICP27 protein enhances gene expression via an interaction with TATA box-binding protein.
Virology
; 324(2): 311-26, 2004 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-15207618
ABSTRACT
The mechanism(s) by which the early EICP27 gene product cooperates with other equine herpesvirus 1 (EHV-1) regulatory proteins to achieve maximal promoter activity remains unknown. Transient transfection assays revealed that deletion of residues 93-140 of the 470-aa EICP27 protein substantially diminished its activation of the immediate-early (IE) promoter, whereas deletion of residues 140-470 that contain a zinc-finger motif abolished this activity. Fluorescence microscopy of cells expressing the full-length EICP27 protein or portions of this protein revealed that an arginine-rich sequence spanning residues 178-185 mediates nuclear entry. Experiments employing the mammalian Gal4 two-plasmid system revealed that the EICP27 protein does not possess an independent trans-activation domain (TAD). Protein-protein interaction assays using purified proteins revealed that residues 124-220 of the EICP27 protein mediate its direct interaction with TATA box-binding protein (TBP). Partial deletion of this TBP-binding domain attenuated the ability of the EICP27 protein to stimulate the IE and early EICP0 promoters by 68% and 71%, respectively, indicating the importance of this protein-protein interaction.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Regulação Viral da Expressão Gênica
/
Herpesvirus Equídeo 1
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Proteína de Ligação a TATA-Box
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Proteínas Virais Reguladoras e Acessórias
Limite:
Animals
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article