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(Received for publication, July 25, 1996, and in revised form, September 17, 1996)
From the Department of Biochemistry and Biophysics, Washington
State University, Pullman, Washington 99164-4660
The promoter for the rat follicle-stimulating
hormone receptor (FSHR) gene contains a conserved consensus
E box sequence and an initiator-like region (InR) sequence.
Deletion analysis and transient transfections showed that a 114-base
pair region (
Volume 271, Number 52,
Issue of December 27, 1996
pp. 33317-33324
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
143 to 30) that encompasses the E box and the InR was
sufficient for greater than 75% of promoter function. DNase I
footprint analysis showed that the E box and InR were protected by
nuclear proteins from rat Sertoli cells, and the E box region was shown
by electrophoretic mobility shift assays (EMSA) to be a site of Sertoli
protein interactions. Mutations in the E box disrupted these
interactions and reduced FSHR promoter activity. Co-transfection of the
nhibitor of 
NA binding (Id) with an
FSHR/luciferase construct into mouse Sertoli 1 cells reduced FSHR
promoter activity. Using EMSA, the upstream stimulatory factor was
shown to be a component of the complexes that interacted with the E box
in the FSHR promoter. Binding of proteins from rat Sertoli cells to the
InR was demonstrated using EMSA. Also, an oligonucleotide that
represented the sequence of the terminal deoxynucleotidyltransferase
InR displaced the complexes at the FSHR InR. Mutations in the InR
resulted in a significant reduction of FSHR promoter activity.
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