A unique thyroid hormone response element in the human immunodeficiency virus type 1 long terminal repeat that overlaps the Sp1 binding sites

28Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free