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(Received for publication, June 12, 1996, and in revised form, August 26, 1996)
From the Departments of In vitro DNA binding
assays and transient transfection analysis with monkey kidney cells
have implicated Nrl, a member of the Maf-Nrl subfamily of bZIP
transcription factors, and the Nrl response element (NRE) in the
regulation of rhodopsin expression. We have now further explored the
role of the NRE and surrounding promoter elements. Using the yeast
one-hybrid screen with integrated NRE and flanking DNA as bait, the
predominant clone obtained was bovine Nrl. Recovery of
truncated clones in the screen demonstrated that the carboxyl-terminal
half of Nrl, which contains the basic and leucine zipper domains, is
sufficient for DNA binding. To functionally dissect the rhodopsin
promoter, transient expression studies with primary chick retinal cell
cultures were performed. Deletion and mutation analyses identified two
positive regulatory sequences: one between
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29612-29618
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
,
,
and§§
Ophthalmology,
Neuroscience, and
§§ Molecular Biology and Genetics, The Johns
Hopkins University School of Medicine,
Baltimore, Maryland 21287-9277, ¶ Departments of Ophthalmology,
Cell Biology, and Anatomy, Cornell University School of Medicine,
New York, New York 10021, and Departments of 
Radiation
Oncology, and ** Ophthalmology and Human Genetics, University of
Michigan, Ann Arbor, Michigan 48105
40 and 84 base pairs
(bp) and another between 84 and 130 bp. Activity of the 40 to
84 region was shown to be largely due to the NRE. On co-transfection
with an NRL expression vector, there were 3-5-fold increases in the
activity of rhodopsin promoter constructs containing an intact NRE but little or no effect with rhodopsin promoters containing a mutated or
deleted NRE. Nrl was more effective than the related bZIP proteins, c-Fos and c-Jun, in stimulating rhodopsin promoter activity. The 84-
to 130-bp region acted synergistically with the NRE to enhance both
the level of basal expression and the degree of Nrl-mediated trans-activation. These studies support Nrl as a regulator of rhodopsin
expression in vivo, identify an additional regulatory region just upstream of the NRE, and demonstrate the utility of primary
retinal cell cultures for characterizing both the cis-acting response
elements and trans-acting factors that regulate photoreceptor gene
expression.
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