Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II.
Open Access
- 15 October 1996
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (21) , 11575-11579
- https://doi.org/10.1073/pnas.93.21.11575
Abstract
Human immunodeficiency virus (HIV)-encoded trans-activator (Tat) acts through the trans-activation response element RNA stem-loop to increase greatly the processivity of RNA polymerase II. Without Tat, transcription originating from the HIV promoter is attenuated. In this study, we demonstrate that transcriptional activation by Tat in vivo and in vitro requires the C-terminal domain (CTD) of RNA polymerase II. In contrast, the CTD is not required for basal transcription and for the formation of short, attenuated transcripts. Thus, trans-activation by Tat resembles enhancer-dependent activation of transcription. These results suggest that effects of Tat on the processivity of RNA polymerase II require proteins that are associated with the CTD and may result in the phosphorylation of the CTD.Keywords
This publication has 21 references indexed in Scilit:
- RNA polymerase II C-terminal domain required for enhancer-driven transcriptionNature, 1995
- The RNA polymerase II holoenzyme and its implications for gene regulationTrends in Biochemical Sciences, 1995
- Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongationNature, 1994
- CONTROL OF RNA INITIATION AND ELONGATION AT THE HIV-1 PROMOTERAnnual Review of Biochemistry, 1994
- Direct interaction of human TFIID with the HIV-1 transactivator TatNature, 1994
- Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: correlations with gene activity and transcript processing.Genes & Development, 1993
- HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors.Genes & Development, 1992
- Two distinct nuclear transcription factors recognize loop and bulge residues of the HIV-1 TAR RNA hairpin.Genes & Development, 1991
- HIV-1 Tat protein increases transcriptional initiation and stabilizes elongationCell, 1989
- Purification using polyethylenimine precipitation and low molecular weight subunit analyses of calf thymus and wheat germ DNA-dependent RNA polymerase IIBiochemistry, 1977