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Equine infectious anemia virus transactivator is a homeodomain-type protein

Journal of Molecular Biology 277(4): 749-755

Equine infectious anemia virus transactivator is a homeodomain-type protein

Lentiviral transactivator (Tat) proteins are essential for viral replication. Tat proteins of human immunodeficiency virus type 1 and bovine immunodeficiency virus form complexes with their respective RNA targets (Tat responsive element, TAR), and specific binding of the equine anemia virus (EIAV) Tat protein to a target TAR RNA is suggested by mutational analysis of the TAR RNA. Structural data on equine infectious anemia virus Tat protein reveal a helix-loop-helix-turn-helix limit structure very similar to homeobox domains that are known to bind specifically to DNA. Here we report results of gel-shift and footprinting analysis as well as fluorescence and nuclear magnetic resonance spectroscopy experiments that clearly show that EIAV Tat protein binds to DNA specifically at the long terminal repeat Pu.1 (GTTCCTGTTTT) and AP-1 (TGACGCG) sites, and thus suggest a common mechanism for the action of some of the known lentiviral Tat proteins via the AP-1 initiator site. Complex formation with DNA induces specific shifts of the proton NMR resonances originating from amino acids in the core and basic domains of the protein.

Accession: 003127921

PMID: 9545368

DOI: 10.1006/jmbi.1998.1636

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Related references

Willbold, D.; Rosin Arbesfeld, P.; Gazit, A.; Yaniv, A.; Frank, R.; Roesch, P., 1994: The solution structure of the transactivator protein of the equine infectious anemia virus. Biological Chemistry Hoppe-Seyler 375(SPEC SUPPL 1): S111

Willbold, D.; Rosin Arbesfeld, R.; Gazit, A.; Yaniv, A.; Frank, R.; Roesch, P., 1993: Structural investigations of the transactivator-protein of the equine infectious anemia virus and its complex to RNA by NMR. Biological Chemistry Hoppe-Seyler 374(9): 685

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