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J Biol Chem, Vol. 273, Issue 21, 13030-13036, May 22, 1998
From the Program in Gene Regulation, Institute of Molecular
Medicine and Genetics, Medical College of Georgia,
Augusta, Georgia 30912
The ability of p53 to induce apoptosis requires
its sequence-specific DNA binding activity; however, the
transactivation-deficient p53(Gln22-Ser23) can still induce
apoptosis. Previously, we have shown that the region between residues
23 and 97 in p53 is necessary for such activity. In an effort to more
precisely map a domain necessary for apoptosis within the N terminus,
we found that deletion of the N-terminal 23 amino acids compromises,
but does not abolish, p53 induction of apoptosis. Surprisingly,
p53(
1-42), which lacks the N-terminal 42 amino acids and the
previously defined activation domain, retains the ability to induce
apoptosis to an even higher level than wild-type p53. A more extensive
deletion, which eliminates the N-terminal 63 amino acids, renders p53
completely inert in mediating apoptosis. In addition, we found that
both p53(1-42) and p53(Gln22-Ser23) can
activate a subset of cellular p53 targets. Furthermore, we showed that
residues 53 and 54 are critical for the apoptotic and transcriptional
activities of both p53(1-42) and
p53(Gln22-Ser23). Taken together, these data
suggest that within residues 43-63 lie an apoptotic domain as well as
another transcriptional activation domain. We therefore postulate that
the apoptotic activity in p53(Gln22-Ser23) and
p53(1-42) is still transcription-dependent.
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