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Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1.

The transcription factor TFII-I has been shown to bind independently to two distinct promoter elements, a pyrimidine-rich initiator (Inr) and a recognition site (E-box) for upstream stimulatory factor 1 (USF1), and to stimulate USF1 binding to both of these sites. Here we describe the isolation of a cDNA encoding TFII-I and demonstrate that the corresponding 120 kDa polypeptide, when expressed ectopically, is capable of binding to both Inr and E-box elements. The primary structure of TFII-I reveals novel features that include six directly repeated 90 residue motifs that each possess a potential helix-loop/span-helix homology. These unique structural features suggest that TFII-I may have the capacity for multiple protein-protein and, potentially, multiple protein-DNA interactions. Consistent with this hypothesis and with previous in vitro studies, we further demonstrate that ectopic TFII-I and USF1 can act synergistically, and in some cases independently, to activate transcription in vivo through both Inr and the E-box elements of the adenovirus major late promoter. We also describe domains of USF1 that are necessary for its independent and synergistic activation functions.

Pubmed ID: 9384587


  • Roy AL
  • Du H
  • Gregor PD
  • Novina CD
  • Martinez E
  • Roeder RG


The EMBO journal

Publication Data

December 1, 1997

Associated Grants

  • Agency: NCI NIH HHS, Id: CA09673
  • Agency: NCI NIH HHS, Id: CA42567
  • Agency: NIAID NIH HHS, Id: F32 AI07696

Mesh Terms

  • Adenoviridae
  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular
  • DNA, Complementary
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • Genes, Reporter
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Protein Binding
  • Recombinant Proteins
  • Repetitive Sequences, Nucleic Acid
  • Transcription Factors
  • Transfection
  • Upstream Stimulatory Factors