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Vol. 12, No. 4, pp. 462-472, February 15, 1998
1 Department of Biological Sciences, Columbia University,
New York, New York 10027 USA;
2 National Institutes of Health,
Building 37, Bethesda, Maryland 20892 USA
The binding of p53 protein to DNA is stimulated by its interaction
with covalent as well as noncovalent modifiers. We report the
identification of a factor from HeLa nuclear extracts that activates
p53 DNA binding. This factor was purified to homogeneity and identified
as the high mobility group protein, HMG-1. HMG-1 belongs to a family of
highly conserved chromatin-associated nucleoproteins that bend DNA and
facilitate the binding of various transcription factors to their
cognate DNA sequences. We demonstrate that recombinant His-tagged HMG-1
enhances p53 DNA binding in vitro and also that HMG-1 and p53 can
interact directly in vitro. Unexpectedly, HMG-1 also stimulates DNA
binding by p53
30, a carboxy-terminally deleted form of the protein
that is considered to be constitutively active, suggesting that HMG-1
stimulates p53 by a mechanism that is distinct from other known
activators of p53. Finally, using transient transfection assays we show
that HMG-1 can increase p53 and p5330-mediated transactivation in
vivo. HMG-1 promotes the assembly of higher order p53 nucleoprotein
structures, and these data, along with the fact that HMG-1 is capable
of bending DNA, suggest that HMG-1 may activate p53 DNA binding by a
novel mechanism involving a structural change in the target DNA.
[Key Words: p53 protein; HMG-1; DNA-binding activation; transcription]
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