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J Biol Chem, Vol. 275, Issue 11, 7619-7625, March 17, 2000
From the Department of Molecular Biology, Parke-Davis
Pharmaceutical Research, Division of Warner-Lambert,
Ann Arbor, Michigan 48105
Transcriptional regulation of many immune
responsive genes is under the control of the transcription factor
NF-
The Structure of the Nuclear Factor-
B Protein-DNA Complex
Varies with DNA-binding Site Sequence*
B. This factor is found in cells as a dimer which can contain any
two members of the Rel family of proteins (p50, p65, p52, c-Rel, and
RelB). The different dimers show distinct preferences for DNA-binding site sequences. To understand the relationship between the DNA binding
properties of the dimer forms and transcriptional activation, the
physical properties of the complexes of p50 and p65 with DNA have been
analyzed. Comparison of apparent DNA binding affinity showed
differences in selectivity of DNA-binding site sequence. The ionic
strength dependence of apparent binding affinity has shown that the
number of ionic interactions in the protein-DNA complex depends on the
DNA-binding site sequence and the dimer form, which are consistent with
changes in the structure of the protein-DNA complex. Using a
fluorescent technique to measure DNA structure changes, protein binding
does not appear to alter the structure of the DNA-binding site within
the limits of detection. These results are consistent with a change in
protein structure that may result in activation differences due to
alternative interactions with other transcription proteins.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 734-622-5090;
Fax: 734-622-5970; E-mail: joseph.menetski@wl.com.
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