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Journal of General Virology, Vol 80, 777-782, Copyright © 1999 by Society for General Microbiology
ARTICLES |
I Choudhury, J Wang, S Stein, A Rabson and MJ Leibowitz
UMDNJ-Robert Wood Johnson Medical School, Department of Molecular Genetics and Microbiology, Piscataway, NJ 08854-5635, USA.
The Tat (trans-activator of transcription) regulatory protein of human immunodeficiency virus (HIV-1) acts by interacting with the TAR RNA domain of nascent viral transcripts and with cellular proteins to increase viral transcription. In Jurkat-derived HCLE-D36 cells, which are stably transfected with the chloramphenicol acetyltransferase (CAT) reporter gene expressed from the TAR-encoding long terminal repeat (LTR) of HIV-1, CAT protein expression is dependent on Tat. The Tat9-K- biotin peptide antagonist of Tat binds specifically to TAR RNA and competes with Tat for binding. In the cellular expression system, Tat9- K-biotin reduces Tat-dependent CAT expression. However, while the Tat antagonist greatly reduces CAT protein production and polysome association of CAT mRNA, it has little effect on CAT mRNA levels, suggesting that the antagonist works at the post-transcriptional level.
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