A Unique Thyroid Hormone Response Element in the Human Immunodeficiency Virus Type 1 Long Terminal Repeat That Overlaps the Sp1 Binding Sites (*)

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.

• Publication year

  1995

• Venue

  Journal of Biological Chemistry

• Publication date

  1995-12-29

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/JBC.270.52.31059PMID 8537364
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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