The Ah receptor (AHR) is a ligand-activated transcription factor that is structurally related to its dimerization partner, the Ah receptor nuclear translocator (ARNT), and two Drosophila proteins, SIM and PER. All four proteins contain a region of homology now referred to as a PAS homology domain. In addition, the AHR, ARNT, and SIM harbor a basic region helix- loop-helix motif in their N termini, whereas PER does not. Previous mapping studies of the AHR have demonstrated that the PAS domain contains sequences required for ligand recognition, dimerization, and interaction with the 90- kDa heat shock protein. They also have confirmed that the basic region helix- loop-helix domain plays a role in both dimerization and sequence-specific DNA binding. To identify domains involved in transactivation of target genes, we generated chimeras of AHR/ARNT deletion mutants with the DNA binding region of the yeast Gal4 protein, transiently expressed these in COS-1 cells, and monitored their capacity to activate the chloramphenicol acetyltransferase reporter gene under the control of a minimal promoter driven by enhancer elements recognized by Gal4. Extensive analysis of these fusions revealed that the AHR and ARNT harbor potent transactivation domains within their C termini. Importantly, the amino-terminal halves of both the AHR and ARNT were found to be devoid of transactivation activity.
|Number of pages||7|
|Journal||Journal of Biological Chemistry|
|State||Published - Dec 16 1994|