Nucleic Acids Research, Vol 27, Issue 15 3205-3212, Copyright © 1999 by Oxford University Press
HI Swanson and JH Yang
Basic helix-loop-helix proteins that interact with the DNA recognition site
CACGTG include the c-Myc/Max heterodimer and the ARNT
(Ahreceptornucleartranslocator) homodimer. We have utilized a PCR-based
protocol to identify high affinity binding sites of either the c- Myc/Max
or ARNT/ARNT dimers and analyzed the ability of these dimers to interact
with their derived consensus sequences and activate genes. chi(2)analysis
of the selected DNA recognition sites revealed that DNA binding of the ARNT
homodimer is symmetric, resulting in the consensus sequence RTCACGTGAY. Gel
shift analysis demonstrated that the flanking nucleotides play an important
role in dictating DNA binding affinity of the ARNT homodimer. These
flanking sequences also regulate the ability of ARNT to competitively
displace the c-Myc/Max heterodimer from a CACGTG-containing sequence.
However, transient transfection analyses in CV-1 cells revealed that ARNT
and c-Myc/Max exhibited similar abilities to activate transcription through
each other's consensus sequences. Taken together, these results indicate
that although binding affinity of these dimers for the CACGTG core
sequences may be differentially influenced by flanking nucleotides,
transcriptional activity may also be determined by other factors, such as
cellular concentrations of these proteins and their co-activators.
ARTICLES
Specificity of DNA binding of the c-Myc/Max and ARNT/ARNT dimers at the CACGTG recognition site
Department of Pharmacology, University of Kentucky, Lexington, KY 40536, USA. hswan@pop.uky.edu
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