FUNCTIONAL DOMAINS REQUIRED FOR TAT-INDUCED TRANSCRIPTIONAL ACTIVATION OF THE HIV-1 LONG TERMINAL REPEAT
FUNCTIONAL DOMAINS REQUIRED FOR TAT-INDUCED TRANSCRIPTIONAL ACTIVATION OF THE HIV-1 LONG TERMINAL REPEAT
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DOI：
10.1002/j.1460-2075.1988.tb03181.x
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发表时间：
1988-10-01
期刊：
影响因子：
11.4
通讯作者：
GAYNOR, RB
中科院分区：
文献类型：
--
作者：
GARCIA, JA;HARRICH, D;GAYNOR, RB
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 identifiy 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.
