       Document 0245
 DOCN  M9640245
 TI    A unique thyroid hormone response element in the human immunodeficiency
       virus type 1 long terminal repeat that overlaps the Sp1 binding sites.
 DT    9604
 AU    Rahman A; Esmaili A; Saatcioglu F; Department of Pharmacology, School of
       Medicine, University of; California, San Diego, La Jolla 92093-0636,
       USA.
 SO    J Biol Chem. 1995 Dec 29;270(52):31059-64. Unique Identifier : AIDSLINE
       MED/96125083
 AB    Long terminal repeat (LTR) of human immunodeficiency virus (HIV) type 1
       is activated by thyroid hormone (T3) receptor alpha (T3R alpha) 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 T3R alpha when linked to a heterologous
       promoter. In addition, the viral transactivator Tat synergizes with T3R
       alpha 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.
 DE    Base Sequence  Binding Sites  Cells, Cultured  DNA-Binding
       Proteins/METABOLISM  Gene Products, tat/METABOLISM  *HIV Long Terminal
       Repeat  Ligands  Molecular Sequence Data  Receptors, Retinoic
       Acid/METABOLISM  Receptors, Thyroid Hormone/METABOLISM  Support,
       Non-U.S. Gov't  Trans-Activators/METABOLISM  Transcription Factor,
       Sp1/*METABOLISM  Transcription Factors/METABOLISM
       Triiodothyronine/*METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

