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Department of Cellular and Structural Biology The University of Texas Health Science Center at San Antonio San Antonio, Texas 78284-7762
The androgen receptor (AR) gene promoter does not
contain the TATA or CAAT box, but it contains a long (
90-bp)
homopurine/homopyrimidine (pur/pyr) stretch immediately upstream of the
Sp1-binding GC box site. This pur/pyr stretch is conserved at the same
proximal position in the rat, mouse, and human AR gene promoters.
Mutation of this region results in a 3-fold decline in promoter
activity, indicating an important regulatory function. Examination of
the conformational state of the AR pur/pyr region with the
single-strand-specific S1 nuclease showed that it is capable of forming
a non-B DNA structure involving unpaired single strands. Fine mapping
of the S1-sensitive site revealed an unsymmetric cleavage pattern
indicative of an intramolecular triple helical H-form DNA conformation.
Electrophoretic mobility shift analyses showed that the pur/pyr region
of the AR promoter can bind a novel pyrimidine single-strand-specific
protein (ssPyrBF) and also a double-strand DNA-binding protein. Both
oligonucleotide cross-competition and antibody supershift experiments
established that the double-strand binding protein is equivalent to
Sp1. Deoxyribonuclease I (DNase I) footprinting analysis showed
multiple Sp1-binding to the pur/pyr site and a weaker Sp1 interaction
to this region compared with the adjacently located GC box, where Sp1
functions to recruit the TFIID complex. These results suggest that the
pur/pyr domain of the AR gene can serve to attract additional Sp1
molecules when it exists in the double-stranded B-DNA conformation.
However, binding of ssPyrBF and the resultant stabilization of the
non-B DNA structure is expected to prevent its interaction with Sp1. We
speculate that in the TATA-less AR gene promoter, multiple weak Sp1
sites at the pur/pyr region adjacent to the GC box can provide a
readily available source of this transcription factor to the functional
GC box, thereby facilitating the assembly of the initiation complex.
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