PMID- 8940186
OWN - NLM
STAT- MEDLINE
DCOM- 19970109
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 49
DP  - 1996 Dec 6
TI  - Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear 
      translocator.
PG  - 31657-65
AB  - The Ah receptor (AHR) and its DNA binding partner, the Ah receptor nuclear 
      translocator (ARNT), are basic helix-loop-helix proteins distinguished by their 
      PER, AHR, ARNT, and SIM (PAS) homology regions. To identify the amino acids of 
      the AHR.ARNT heterodimer that contact the TNGCGTG recognition sequence, we have 
      performed deletion mapping and amino acid substitutions within the N termini of 
      both the AHR and ARNT. The ability of the variant AHR and ARNT proteins to bind 
      DNA and activate gene transcription was determined by the gel shift analysis and 
      transient transfection assays. We have found that the amino acids of ARNT that 
      contact DNA are similar to those of other basic/helix-loop-helix proteins and 
      include glutamic acid residue 83 and arginine residues 86 and 87. Although our 
      initial experiments indicated that DNA binding of the AHR may involve two regions 
      that are bordered by amino acids 9-17 and amino acids 34-42, further analysis 
      demonstrated that only amino acids 34-39 are critical for the AHR.TNGC 
      interaction. These experiments indicate that while the structural features of the 
      ARNT.GTG complex may closely resemble that deduced for proteins such as Max, E47, 
      and USF, the AHR.TNGC complex may represent a unique DNA binding form of 
      basic/helix-loop-helix proteins.
FAU - Swanson, H I
AU  - Swanson HI
AD  - Department of Pharmacology, University of Kentucky, University of Kentucky 
      Medical Center, Lexington, Kentucky 40536, USA. hswan@pop.uky.edu
FAU - Yang, J h
AU  - Yang Jh
LA  - eng
GR  - R29 ES008088/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Receptors, Aryl Hydrocarbon)
RN  - 0 (Transcription Factors)
RN  - 138391-32-9 (Aryl Hydrocarbon Receptor Nuclear Translocator)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Amino Acid Sequence
MH  - Aryl Hydrocarbon Receptor Nuclear Translocator
MH  - DNA/*metabolism
MH  - *DNA-Binding Proteins
MH  - *Helix-Loop-Helix Motifs
MH  - Molecular Sequence Data
MH  - Plasmids/metabolism
MH  - Polymerase Chain Reaction
MH  - Protein Conformation
MH  - Receptors, Aryl Hydrocarbon/*metabolism
MH  - Transcription Factors/*metabolism
MH  - Transcription, Genetic
EDAT- 1996/12/06 00:00
MHDA- 1996/12/06 00:01
CRDT- 1996/12/06 00:00
PHST- 1996/12/06 00:00 [pubmed]
PHST- 1996/12/06 00:01 [medline]
PHST- 1996/12/06 00:00 [entrez]
AID - S0021-9258(19)79039-5 [pii]
AID - 10.1074/jbc.271.49.31657 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Dec 6;271(49):31657-65. doi: 10.1074/jbc.271.49.31657.