The VP16 transcription activation domain is functional when targeted to a promoter-proximal RNA sequence.
Journal Article (Journal Article)
Among eukaryotic transcription trans-activators, the human immunodeficiency virus type 1 (HIV-1) Tat protein is exceptional in that its target site TAR is an RNA rather than a DNA sequence. Here, we confirm that fusion of Tat to the RNA-binding domain of the HIV-1 Rev protein permits the efficient activation of an HIV-1 long terminal repeat (LTR) promoter in which critical TAR sequences have been replaced by RNA sequences derived from the HIV-1 Rev response element (RRE). An RRE target sequence as small as 13 nucleotides is shown to form an effective in vivo target for Rev binding. More important, a fusion protein consisting of Rev attached to the VP16 transcription activation domain was also observed to efficiently activate the HIV-1 LTR from this nascent RNA target. These data demonstrate that trans-activation of transcription by acidic activation domains does not require a stable interaction with the promoter DNA and suggest that VP16, like Tat, can act on steps subsequent to the formation of the HIV-1 LTR preinitiation complex. The finding that the activation domains of VP16 and Tat are functionally interchangeable raises the possibility that these apparently disparate viral trans-activators may nevertheless act via similar mechanisms.
Full Text
Duke Authors
Cited Authors
- Tiley, LS; Madore, SJ; Malim, MH; Cullen, BR
Published Date
- November 1992
Published In
Volume / Issue
- 6 / 11
Start / End Page
- 2077 - 2087
PubMed ID
- 1427073
International Standard Serial Number (ISSN)
- 0890-9369
Digital Object Identifier (DOI)
- 10.1101/gad.6.11.2077
Language
- eng
Conference Location
- United States