cDNA cloning and structure of mouse putative Ah receptor

Biochem Biophys Res Commun. 1992 Apr 15;184(1):246-53. doi: 10.1016/0006-291x(92)91185-s.

Abstract

Mouse cDNA clones for a putative Ah receptor have been isolated from a cDNA library of mRNA from Hepa-1 cells by an oligonucleotide probe produced by PCR with a pair of primers which was synthesized according to the reported N-terminal sequence of 26 amino acids. The cDNA clones encode a polypeptide of 805 amino acids with a helix-loop-helix motif and with some similarity to a certain region designated PAS of Drosophila Per and Sim, and human Arnt protein. Cotransfection of an expression vector of the Ah receptor with a reporter plasmid pMC6.3k consisting of CYP1A1 promoter and CAT structural gene into CV-1 cells enhanced the CAT expression in response to added 3-methylcholanthrene.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Chloramphenicol O-Acetyltransferase / genetics
  • Chloramphenicol O-Acetyltransferase / metabolism
  • Cloning, Molecular
  • Gene Library
  • Humans
  • Methylcholanthrene / pharmacology
  • Mice
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Polychlorinated Dibenzodioxins / metabolism
  • Polymerase Chain Reaction
  • Receptors, Aryl Hydrocarbon
  • Receptors, Drug / genetics*
  • Recombinant Fusion Proteins / metabolism
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Transfection

Substances

  • Oligonucleotide Probes
  • Polychlorinated Dibenzodioxins
  • Receptors, Aryl Hydrocarbon
  • Receptors, Drug
  • Recombinant Fusion Proteins
  • Methylcholanthrene
  • Chloramphenicol O-Acetyltransferase