Functional domains of the simian foamy virus type 1 transcriptional transactivator (Taf)

Abstract

The genome of simian foamy virus type 1 encodes a transcriptional transactivator (Taf) that dramatically elevates gene expression directed by the viral long terminal repeat. In this report, we describe the functional domains of simian foamy virus type 1 Taf. Several taf mutants and fusion proteins of Taf and the DNA-binding domain of the Saccharomyces cerevisiae transcriptional transactivator GAL4 were used in this study. Taf contains two potent activation domains. One of the activation domains is located at the amino terminus (positions 1 to 48, with position 1 representing the initiator amino acid methionine) and contains several acidic amino acids. The second activation domain was mapped to a region at the carboxy terminus (positions 277 to 300). These two domains activate gene expression directed by the viral long terminal repeat independently of each other. No significant amino acid sequence homology between the activation domains is noted. Thus, Taf belongs in part to the family of acidic transcriptional transactivators. The activation domain at the carboxy terminus is conserved among foamy virus transactivators but is not related to other known transcriptional activators. Therefore, the mechanism of gene activation by the carboxy terminus of Taf may be novel. In addition, a potential binding domain rich in basic amino acids (positions 179 to 222) and a highly conserved sequence among foamy virus transactivators (positions 93 to 109) were found to be critical for Taf activity.