Limited proteolytic digestions identify common structural features of HIV-1 Tat proteins expressed during infection from alternatively spliced mRNAs
Article Abstract:
A structural analysis of three Tat proteins from a strain of HIV is presented. Tat is one of nine known HIV proteins and plays a key role in HIV replication. Many forms of the Tat protein exist because of alternative splicing of the HIV messenger RNA. The three forms examined - the 86R Tat, the 72R Tat and the Tev protein - all have full transactivation activity. Structural analysis indicated that the first exon in all three proteins is folded into a similar structure. There was no evidence of any subdomains within first exon. These findings suggest that the transactivation function may be contained in a single, common biochemical domain. Although this analysis was conducted on laboratory-grown cells, considerable evidence shows that these proteins assume the same conformation and without need for additional factors in the body.
Publication Name: Journal of Acquired Immune Deficiency Syndromes
Subject: Health
ISSN: 0894-9255
Year: 1993
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Mutational analysis of the amino and carboxy termini of the HIV-2 Tat protein
Article Abstract:
Genetic analysis of a protein in one of the viruses that causes AIDS, HIV-2, can identify which components are necessary for viral reproduction. The regulator protein, or Tat-2, is essential to the replication of the virus. A structural analysis found molecular similarities with the regulator protein Tat-1 found in HIV-1. Mapping of the first coding sequence of the gene identified 99 molecular residues. Deletion of the sequence from eight to 47 stopped reproductive activity. Deletion of the sequence eight through 33 dramatically lowered the activity. Compounds that are able to inhibit Tat action may be able to stop replication of the virus.
Publication Name: Journal of Acquired Immune Deficiency Syndromes
Subject: Health
ISSN: 0894-9255
Year: 1993
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Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro
Article Abstract:
The binding of the HIV viral Tat protein appears to be independent of the site involved in the activation of viral reproduction. An experiment revealed that the activation site alone binds to the human TATA-binding protein (TBP) just as full-length Tat does. Even a mutant Tat protein that could no longer activate viral reproduction was capable of binding to TBP. However, this was only true if the H1 alpha helical region in the carboxy terminus was intact.
Publication Name: Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology
Subject: Health
ISSN: 1077-9450
Year: 1996
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