Identification of cellular protein that can interact specifically with the basic helix-loop-helix domain of the aromatic hydrocarbon receptor.
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.
Hossain
A
A
Department of Molecular Genetics, Tohoku University, Sendai, Japan.
Kikuchi
H
H
Ikawa
S
S
Sagami
I
I
Watanabe
M
M
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D005982:Glutathione Transferase / Q000235:genetics; D018257:Helix-Loop-Helix Motifs; D015151:Immunoblotting; D008099:Liver / Q000737:chemistry; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D008970:Molecular Weight; D000072317:Polychlorinated Dibenzodioxins / Q000494:pharmacology; D011506:Proteins / Q000378:metabolism*; D018336:Receptors, Aryl Hydrocarbon / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins
D000072317:Polychlorinated Dibenzodioxins; D011506:Proteins; D018336:Receptors, Aryl Hydrocarbon; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase