The activation region of the Tat protein of human immunodeficiency virus type-1 functions in yeast.

The N-terminal 48 amino acids of the Tat protein of human immunodeficiency virus type (HIV)-1 constitute its activation region. This region can autonomously activate transcription when targeted to the HIV-1 long terminal repeat or certain heterologous promoters either through DNA binding sites located upstream of the transcription initiation site or via downstream RNA binding sites in mammalian cells. To determine whether the Tat activation region can function in yeast, we have assayed the effect of a chimeric gene (GAL-Tat48) expressing the DNA binding domain of the yeast transcription factor Gal4 (residues 1-147) and the activation region of Tat on GAL1 promoter-directed expression of the lacZ reporter gene in Saccharomyces cerevisiae. Our results indicate that the Gal-Tat48 fusion protein can induce significant activation of the GAL1 promoter. Analysis of a number of Tat mutants located within the activation region indicate that the amino acid residues of Tat essential for trans-activation in mammalian cells are also required for transactivation in yeast. Our results suggest that Tat-mediated transcriptional activation may involve a mechanism conserved among yeast and mammalian cells.