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Volume 272, Number 52, Issue of December 26, 1997 pp. 33132-33139
B p52 Homodimer Binding to DNA
(Received for publication, August 12, 1997, and in revised form, October 17, 1997)
From the Departments of Pathology and of Radiation and Cellular
Oncology, University of Chicago, Chicago, Illinois 60637
I
B proteins control the subcellular
localization and DNA binding activity of NF-
B transcription factors.
BCL3 is a nuclear I
B that can inhibit or enhance the binding of
NF-
B p50 or p52 homodimers to consensus DNA-binding (
B) sequences
or form a
B-binding complex with homodimers. To study BCL3 function,
we have used gel shift analysis and tagged protein and tagged DNA
coprecipitation analyses. Our results show that at intermediate ratios
of BCL3 to p52 all observed phosphoforms of BCL3 are able to form a
B-binding complex with p52 homodimers. At low BCL3/p52 ratios, BCL3
increases the rate of p52 homodimer binding to
B sites in the
presence of nonconsensus DNA and dissociates from the complex. At high BCL3/p52 ratios, BCL3 forms a higher order inhibitory complex with p52
homodimers. All of these effects depend on BCL3 phosphorylation and
relative concentration. These results indicate that BCL3
phosphorylation may affect its regulation of
NF-
B-dependent transcription in vivo.
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