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. 1988 Oct;7(10):3143-7.
doi: 10.1002/j.1460-2075.1988.tb03181.x.

Functional domains required for tat-induced transcriptional activation of the HIV-1 long terminal repeat

J A Garcia  1 , D Harrich, L Pearson, R Mitsuyasu, R B Gaynor
Affiliations

Functional domains required for tat-induced transcriptional activation of the HIV-1 long terminal repeat

J A Garcia et al. EMBO J. 1988 Oct.

Abstract

The transcriptional regulation of the human immunodeficiency virus (HIV) type I involves the interaction of both viral and cellular proteins. The viral protein tat is important in increasing the amount of viral steady-state mRNA and may also play a role in regulating the translational efficiency of viral mRNA. To identify distinct functional domains of tat, oligonucleotide-directed mutagenesis of the tat gene was performed. Point mutations of cysteine residues in three of the four Cys-X-X-Cys sequences in the tat protein resulted in a marked decrease in transcriptional activation of the HIV long terminal repeat. Point mutations which altered the basic C-domain of the protein also resulted in decreases in transcriptional activity, as did a series of mutations that repositioned either the N or C termini of the protein. Conservative mutations of other amino acids in the cysteine-rich or basic regions and in a series of proline residues in the N terminus of the molecule resulted in minimal changes in tat activation. These results suggest that several domains of tat protein are involved in transcriptional activation with the cysteine-rich domain being required for complete activity of the tat protein.

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