PMID- 7989319
OWN - NLM
STAT- MEDLINE
DCOM- 19950112
LR  - 20210212
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 50
DP  - 1994 Dec 16
TI  - Potent transactivation domains of the Ah receptor and the Ah receptor nuclear 
      translocator map to their carboxyl termini.
PG  - 31518-24
AB  - 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.
FAU - Jain, S
AU  - Jain S
AD  - Department of Molecular Pharmacology and Biological Chemistry, Northwestern 
      University Medical School, Chicago, Illinois 60611.
FAU - Dolwick, K M
AU  - Dolwick KM
FAU - Schmidt, J V
AU  - Schmidt JV
FAU - Bradfield, C A
AU  - Bradfield CA
LA  - eng
GR  - ES05703/ES/NIEHS NIH HHS/United States
GR  - T32 CA09560/CA/NCI NIH HHS/United States
GR  - T32 ES07124/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Arnt protein, mouse)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Receptors, Aryl Hydrocarbon)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
RN  - 138391-32-9 (Aryl Hydrocarbon Receptor Nuclear Translocator)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Aryl Hydrocarbon Receptor Nuclear Translocator
MH  - Base Sequence
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - DNA Mutational Analysis
MH  - *DNA-Binding Proteins
MH  - *Gene Expression Regulation
MH  - In Vitro Techniques
MH  - Mice
MH  - Molecular Sequence Data
MH  - Oligodeoxyribonucleotides/chemistry
MH  - Receptors, Aryl Hydrocarbon/*chemistry
MH  - Recombinant Fusion Proteins
MH  - Recombinant Proteins
MH  - Structure-Activity Relationship
MH  - Trans-Activators/*chemistry
MH  - Transcription Factors/*chemistry
EDAT- 1994/12/16 00:00
MHDA- 1994/12/16 00:01
CRDT- 1994/12/16 00:00
PHST- 1994/12/16 00:00 [pubmed]
PHST- 1994/12/16 00:01 [medline]
PHST- 1994/12/16 00:00 [entrez]
AID - S0021-9258(18)31725-3 [pii]
PST - ppublish
SO  - J Biol Chem. 1994 Dec 16;269(50):31518-24.