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J. Biol. Chem., Vol. 275, Issue 51, 39944-39953, December 22, 2000
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From the Department of Biological Sciences, Columbia University,
New York, New York 10027
It is important to gain insight into p53 DNA
binding and how it is regulated. By using electrophoretic mobility
shift assays and DNase I footprinting, we show that a region within the
N terminus of the protein controls the dissociation of p53 from a
p53-binding site. When p53 is bound by a number of N-terminal-specific
monoclonal antibodies, its rate of dissociation from DNA is reduced,
and its ability to protect a cognate site from DNase I digestion is increased. Moreover, greatly reduced dissociation is observed with p53
protein lacking the N-terminal 96 amino acids. By contrast, deletion of
the C terminus does not affect p53 dissociation from DNA or DNase I
protection. p53 protein expressed in and purified from bacterial cells
displays markedly more instability on its consensus DNA-binding site
than does p53 produced in insect cells, suggesting that
post-translational modifications may affect the stability of the
protein. Our results provide evidence that the N terminus of p53
possesses an auto-inhibitory function that is mechanistically different
from the inhibitory region at the C terminus.
The N Terminus of p53 Regulates Its Dissociation from DNA*
*
This work was supported by National Institutes of Health
Grant CA77742.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.: 212-854-2557;
Fax: 212-865-8246; E-mail: clp3@columbia.edu.
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