Long terminal repeat (LTR) of human immunodeficiency virus (HIV) type 1 is activated by thyroid hormone (T3) receptor α (T3Rα) in the absence of ligand. Addition of T3 reverses this effect. This activity is mediated by a high affinity T3 response element (T3RE) within the HIV-1 LTR, termed the HIV-T3RE (bases -74 to -50), which coincides with the Sp1 element as demonstrated by mobility shift, DNaseI footprinting, and methylation interference analyses. HIV-T3RE mediates ligand-independent activation of transcription by T3Rα when linked to a heterologous promoter. In addition, the viral transactivator Tat synergizes with T3Rα to activate the HIV-1 LTR in the absence of T3, which is relieved in its presence. These findings have implications for the possible control of HIV-1 LTR activity by T3.
CITATION STYLE
Rahman, A., Esmaili, A., & Saatcioglu, F. (1995). A unique thyroid hormone response element in the human immunodeficiency virus type 1 long terminal repeat that overlaps the Sp1 binding sites. Journal of Biological Chemistry, 270(52), 31059–31064. https://doi.org/10.1074/jbc.270.52.31059
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