PMID- 7592839
OWN - NLM
STAT- MEDLINE
DCOM- 19951221
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 270
IP  - 44
DP  - 1995 Nov 3
TI  - DNA binding specificities and pairing rules of the Ah receptor, ARNT, and SIM 
      proteins.
PG  - 26292-302
AB  - The Ah receptor (AHR), the Ah receptor nuclear translocator protein (ARNT), and 
      single-minded protein (SIM) are members of the basic helix-loop-helix-PAS 
      (bHLH-PAS) family of regulatory proteins. In this study, we examine the DNA 
      half-site recognition and pairing rules for these proteins using oligonucleotide 
      selection-amplification and coprecipitation protocols. Oligonucleotide 
      selection-amplification revealed that a variety of bHLH-PAS protein combinations 
      could interact, with each generating a unique DNA binding specificity. To 
      validate the selection-amplification protocol, we demonstrated the preference of 
      the AHR.ARNT complex for the sequence commonly found in dioxin-responsive 
      enhancers in vivo (TNGCGTG). We then demonstrated that the ARNT protein is 
      capable of forming a homodimer with a binding preference for the palindromic 
      E-box sequence, CACGTG. Further examination indicated that ARNT may have a 
      relaxed partner specificity, since it was also capable of forming a heterodimer 
      with SIM and recognizing the sequence GT(G/A)CGTG. Coprecipitation experiments 
      using various PAS proteins and ARNT were consistent with the idea that the ARNT 
      protein has a broad range of interactions among the bHLH-PAS proteins, while the 
      other members appear more restricted in their interactions. Comparison of this in 
      vitro data with sites known to be bound in vivo suggests that the high affinity 
      half-site recognition sequences for the AHR, SIM, and ARNT are T(C/T)GC, GT(G/A)C 
      (5'-half-sites), and GTG (3'-half-sites), respectively.
FAU - Swanson, H I
AU  - Swanson HI
AD  - Department of Molecular Pharmacology and Biological Chemistry, Northwestern 
      University Medical School, Chicago, Illinois 60611, USA.
FAU - Chan, W K
AU  - Chan WK
FAU - Bradfield, C A
AU  - Bradfield CA
LA  - eng
GR  - F32 ES005589/ES/NIEHS NIH HHS/United States
GR  - ES-05589/ES/NIEHS NIH HHS/United States
GR  - ES-05660/ES/NIEHS NIH HHS/United States
GR  - ES-05703/ES/NIEHS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
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 (Basic Helix-Loop-Helix Transcription Factors)
RN  - 0 (DNA Probes)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Receptors, Aryl Hydrocarbon)
RN  - 0 (Transcription Factors)
RN  - 0 (sim protein, Drosophila)
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  - Basic Helix-Loop-Helix Transcription Factors
MH  - Cell-Free System
MH  - Consensus Sequence
MH  - DNA Probes
MH  - DNA-Binding Proteins/biosynthesis/*metabolism
MH  - Drosophila Proteins
MH  - Gene Expression Regulation
MH  - Helix-Loop-Helix Motifs
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/biosynthesis/*metabolism
MH  - Oligodeoxyribonucleotides/chemical synthesis/metabolism
MH  - Protein Biosynthesis
MH  - Rabbits
MH  - Receptors, Aryl Hydrocarbon/biosynthesis/*metabolism
MH  - Reticulocytes/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Transcription Factors/biosynthesis/*metabolism
EDAT- 1995/11/03 00:00
MHDA- 1995/11/03 00:01
CRDT- 1995/11/03 00:00
PHST- 1995/11/03 00:00 [pubmed]
PHST- 1995/11/03 00:01 [medline]
PHST- 1995/11/03 00:00 [entrez]
AID - S0021-9258(18)92477-4 [pii]
AID - 10.1074/jbc.270.44.26292 [doi]
PST - ppublish
SO  - J Biol Chem. 1995 Nov 3;270(44):26292-302. doi: 10.1074/jbc.270.44.26292.