Jm. Kim et al., Transactivation activity of the human cytomegalovirus IE2 protein occurs at steps subsequent to TATA box-binding protein recruitment, J GEN VIROL, 81, 2000, pp. 37-46
The IE2 protein of human cytomegalovirus transactivates viral and cellular
promoters through a wide variety of cis-elements, but the mechanism of its
action has not been well characterized. Here, IE2-Sp1 synergy and IE2-TATA
box-binding protein (TBP) interaction are examined by artificial recruitmen
t of either Sp1 or TBP to the promoter. It was found that IE2 could coopera
te with DNA-bound Sp1.A 117 amino acid glutamine-rich fragment of Sp1, whic
h can interact with Drosophila TAF(II)110 and human TAF(II)130, was suffici
ent for the augmentation of IE2-driven transactivation. In binding assays i
n vitro, IE2 interacted directly with the C-terminal region of Sp1,which co
ntains the zinc finger DNA-binding domain, but not with its transactivation
domain, suggesting that synergy between IE2 and the transactivation domain
of Sp1 might be mediated by other proteins such as TAF or TBP. It was also
found that TBP recruitment to the promoter markedly increased IE2-mediated
transactivation. Thus, IE2 acts synergistically with DNA-bound Sp1 and DNA
-bound TBP. These results suggest that, in human cytomegalovirus IE2 transa
ctivation, Sp1 functions at an early step such as recruitment of TBP and IE
2 acts to accelerate rate-limiting steps after TBP recruitment.