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(Received for publication, June 15, 1995; and in revised form, August 4, 1995) Tumor suppressor protein p53 is a potent transcriptional
activator and regulates cell growth negatively. To characterize the
transcriptional activation domain (TAD) of p53, various point mutants
were constructed in the context of Gal4 DNA binding domain and tested
for their transactivation ability. Our results demonstrated that the
positionally conserved hydrophobic residues shared with herpes simplex
virus VP16 and other transactivators are essential for transactivation.
Also, the negatively charged residues and proline residues are
necessary for full activity, but not essential for the activity of p53
TAD. Deletion analyses showed that p53 TAD can be divided into two
subdomains, amino acids 1-40 and 43-73. An in vitro glutathione S-transferase pull-down assay establishes a
linear correlation between p53 TAD-mediated transactivation in vivo and the binding activity of p53 TAD to TATA-binding protein (TBP) in vitro. Mutations that diminish the transactivation ability
of Gal4-p53 TAD also impair the binding activity to TBP severely. Our
results suggest that at least TBP is a direct target for p53 TAD and
that the binding strength of TAD to TBP (TFIID) is an important
parameter controlling activity of p53 TAD. In addition, circular
dichroism spectroscopy has shown that p53 TAD peptide lacks any regular
secondary structure in solution and that there is no significant
difference between the spectra of the wild type TAD and that of the
transactivation-deficient mutant type.
Volume 270,
Number 42,
Issue of October 20, 1995 pp. 25014-25019
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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