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J Biol Chem, Vol. 273, Issue 29, 18538-18546, July 17, 1998
Nuclear Factor I (NFI) Isoforms Differentially Activate
Simple versus Complex NFI-responsive Promoters
Ali Z.
Chaudhry ,
Alfredo D.
Vitullo§, and
Richard M.
Gronostajski §
From the Department of Biochemistry, Case Western
Reserve University, Cleveland, Ohio 44106 and the
§ Department of Cancer Biology, Lerner Research Institute,
Cleveland Clinic Foundation, Cleveland, Ohio 44195
Promoter-specific differences in the function of
transcription factors play a central role in the regulation of gene
expression. We have measured the maximal transcriptional activation
potentials of nuclear factor I (NFI) proteins encoded by each of the
four identified NFI genes (NFI-A, -B, -C, and -X) by transient
transfection in JEG-3 cells using two model NFI-dependent
promoters: 1) a simple chimeric promoter containing a single
NFI-binding site upstream of the adenovirus major late promoter
(NFI-Ad), and 2) the more complex mouse mammary tumor virus long
terminal repeat promoter. The relative activation potentials for the
NFI isoforms differed between the two promoters, with NFI-X being the
strongest activator of NFI-Ad and NFI-B being the strongest activator
of the MMTV promoter. To determine if these promoter-specific
differences in activation potential were due to the presence of
glucocorticoid response elements (GREs), we added GREs upstream of the
NFI-binding site in NFI-Ad. NFI-X remains the strongest activator of
the GRE containing simple promoter, indicating that differences in
relative activation potential are not due solely to the presence of
GREs. Since NFI proteins bind to DNA as dimers, we assessed the
activation potentials of NFI heterodimers. Here, we show that NFI
heterodimers have intermediate activation potentials compared with
homodimers, demonstrating one potential mechanism by which different
NFI proteins can regulate gene expression.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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