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(Received for publication, August 5, 1996, and in revised form, October 4, 1996)
From the Department of Genetics, Molecular and General Biology,
University of Naples "Federico II," via Mezzocannone 8, 80134 Naples and International Institute of Genetics and Biophysics, CNR, via
Marconi 10, 80125 Naples, Italy
Sp3 is a member of the Sp family of transcription
factors and binds to DNA with affinity and specificity comparable to
that of Sp1. We demonstrate that Sp3 is a bifunctional transcription factor that can both activate and repress transcription. Gene fusion
experiments in mammalian cells demonstrate that the Sp3 activation
potential is distributed over an extensive glutamine-rich N-terminal
region, whereas the repressor activity has been mapped in a 72-amino
acid region located at the 5
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4021-4026
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
of the zinc finger DNA-binding domain. We
demonstrated that the repression activity is strictly dependent on the
context of the DNA-binding sites bound by Sp3. We found that Sp3
represses transcription of promoters bearing multiple GAL4 DNA-binding
sites, whereas it activates isogenic reporters containing a single
GAL4-binding site. Transfection experiments in Drosophila
cells that lack endogenous Sp activity demonstrated that Sp3 does not
possess an active repression domain that can function in insect cells,
rather it is a weak transcriptional activator of the c-myc
promoter. Our results strongly suggest that Sp3 is a dual-function
regulator whose activity is dependent upon both the promoter and the
cellular context.
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