Nucleic Acids Research, Vol 25, Issue 19 3895-3903, Copyright © 1997 by Oxford University Press
P Tarapore, C Richmond, G Zheng, SB Cohen, B Kelder, J Kopchick, U Kruse, AE Sippel, C Colmenares and E Stavnezer
The Ski oncoprotein has been found to bind non-specifically to DNA in
association with unindentified nuclear factors. In addition, Ski has been
shown to activate transcription of muscle-specific and viral
promoters/enhancers. The present study was undertaken to identify Ski's DNA
binding and transcriptional activation partners by identifying specific DNA
binding sites. We used nuclear extracts from a v-Ski- transduced mouse
L-cell line and selected Ski-bound sequences from a pool of degenerate
oligonucleotides with anti-Ski monoclonal antibodies. Two sequences were
identified by this technique. The first (TGGC/ANNNNNT/GCCAA) is the
previously identified binding site of the nuclear factor I (NFI) family of
transcription factors. The second (TCCCNNGGGA) is the binding site of
Olf-1/EBF. By electophoretic mobility shift assays we find that Ski is a
component of one or more NFI complexes but we fail to detect Ski in
Olf-1/EBF complexes. We show that Ski binds NFI proteins and activates
transcription of NFI reporters, but only in the presence of NFI. We also
find that homodimerization of Ski is essential for co-activation with NFI.
However, the C-terminal dimerization domain of c-Ski, which is missing in
v-Ski, can be substituted by the leucine zipper domain of GCN4.
ARTICLES
DNA binding and transcriptional activation by the Ski oncoprotein mediated by interaction with NFI
Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.
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