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Major product pp43 of human cytomegalovirus U(L)112-113 gene is a transcriptional coactivator with two functionally distinct domains.

Abstract：

:Human cytomegalovirus U(L)112-113 encodes four phosphoproteins, pp84, pp50, pp43, and pp34, with common amino-termini. A previous report by Kerry et al. (J. Virol. 70, 373-382, 1996) demonstrated that U(L)112-113 products activate U(L)54 promoter in cooperation with immediate-early (IE) proteins. In this study, we identified a domain required for transcriptional activation in the pp43 protein, which consisted of two distinct regions: domain I (amino acids 272-296) and domain II (amino acids 297-306). Domain I contained two long glycine stretches, and domain II was a short proline-containing region. Both of domains were required for IE2-dependent transcriptional activation. The pp43 mutant that had domain I but lacked domain II acted as a dominant negative mutant and suppressed most of the IE2-dependent activation, indicating the importance of coactivation by pp43 in this transcriptional activation. The major protein pp43 also weakly activated the promoter through IR1 element in a manner independent of IE2. Only domain I was required for this IE2-independent activation. These domains were common in pp84, pp50, and pp43 but did not exist in pp34, which did not activate transcription alone. These results suggest that the major product, pp43, of U(L)112-113 has two functionally distinct domains and plays an important role in mediating IE2-dependent transcriptional activation.

journal_name

Virology

journal_title

Virology

authors

Li J,Yamamoto T,Ohtsubo K,Shirakata M,Hirai K

doi

10.1006/viro.1999.9800

subject

Has Abstract

pub_date

1999-07-20 00:00:00

pages

89-97

issue

1

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(99)99800-8

journal_volume

260

pub_type

杂志文章

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