Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins.
Journal Article (Journal Article)
Transcriptional activation of HIV-1 gene expression by the viral Tat protein requires the interaction of a cellular cofactor with the Tat activation domain. This domain has been shown to consist of the cysteine-rich and core motifs of HIV-1 Tat and is functionally conserved in the distantly related Tat proteins of HIV-2 and EIAV. Using the yeast two-hybrid system, we have identified a novel human gene product, termed HT2A, that specifically and precisely binds to the activation domain of HIV-1 Tat and that can also interact with the HIV-2 and EIAV Tat proteins in vivo. We present data further demonstrating that the interaction between the activation domain of HIV-1 Tat and the HT2A protein can be readily detected in the mammalian cell nucleus. Sequence analysis demonstrates that HT2A is a novel member of the C3HC4 or ring finger family of zinc finger proteins that includes several known oncogenes and transcription factors. Overall, these data suggest that HT2A may play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo.
Full Text
Duke Authors
Cited Authors
- Fridell, RA; Harding, LS; Bogerd, HP; Cullen, BR
Published Date
- June 1, 1995
Published In
Volume / Issue
- 209 / 2
Start / End Page
- 347 - 357
PubMed ID
- 7778269
International Standard Serial Number (ISSN)
- 0042-6822
Digital Object Identifier (DOI)
- 10.1006/viro.1995.1266
Language
- eng
Conference Location
- United States