Identification of Cellular Protein That Can Interact Specifically with the Basic Helix-Loop-Helix Domain of the Aromatic Hydrocarbon Receptor

A. Hossain, H. Kikuchi, Shuntaro Ikawa, I. Sagami, M. Watanabe

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The Ah receptor is a basic helix-loop-helix (bHLH)-PAS protein and functions as a ligand-activated DNA binding protein directly interacting with target genes by binding to xenobiotic responsive elements. We have sought to identify possible cellular proteins that can interact with the Ah receptor. The bHLH domain of the Ah receptor was fused to glutathione-S-transferase (GST), and the resulting fusion protein was used as a probe to help us to identify receptor associated protein(s). At least one such protein, 45kDa (p45), was detected in mouse liver extracts, but it does not bind to the bHLH domain of the Ah receptor nuclear translocator, nor to the transactivation domain of Ah receptor or GST alone.

Original languageEnglish
Pages (from-to)405-411
Number of pages7
JournalBiochemical and biophysical research communications
Volume215
Issue number1
DOIs
Publication statusPublished - 1995 Oct 4

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Identification of Cellular Protein That Can Interact Specifically with the Basic Helix-Loop-Helix Domain of the Aromatic Hydrocarbon Receptor'. Together they form a unique fingerprint.

  • Cite this