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Molecular and Cellular Biology, February 1999, p. 1092-1100, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Two Polymorphic Variants of Wild-Type p53 Differ Biochemically and Biologically

Miranda Thomas,1 Ann Kalita,2 Sylvie Labrecque,2 David Pim,1 Lawrence Banks,1,* and Greg Matlashewski2,3,*

International Centre for Genetic Engineering and Biotechnology, I-34012 Trieste, Italy,1 and Institute of Parasitology2 and McGill Cancer Center,3 McGill University, Montreal, Canada

Received 14 May 1998/Returned for modification 3 July 1998/Accepted 29 October 1998

The wild-type p53 protein exhibits a common polymorphism at amino acid 72, resulting in either a proline residue (p53Pro) or an arginine residue (p53Arg) at this position. Despite the difference that this change makes in the primary structure of the protein resulting in a difference in migration during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, no differences in the biochemical or biological characteristics of these wild-type p53 variants have been reported. We have recently shown that p53Arg is significantly more susceptible than p53Pro to the degradation induced by human papillomavirus (HPV) E6 protein. Moreover, this may result in an increased susceptibility to HPV-induced tumors in homozygous p53Arg individuals. In further investigating the characteristics of these p53 variants, we now show that both forms are morphologically wild type and do not differ in their ability to bind to DNA in a sequence-specific manner. However, there are a number of differences between the p53 variants in their abilities to bind components of the transcriptional machinery, to activate transcription, to induce apoptosis, and to repress the transformation of primary cells. These observations may have implications for the development of cancers which harbor wild-type p53 sequences and possibly for the ability of such tumors to respond to therapy, depending on their p53 genotype.

* Corresponding author. Mailing address for Lawrence Banks: International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy. Phone: 39 40 375 7328. Fax: 39 40 226555. E-mail: banks{at}icgeb.trieste.it. Mailing address for Greg Matlashewski: Institute of Parasitology, Macdonald Campus, McGill University, Montreal, Quebec H9X 3V9, Canada. Phone: (514) 398-7727. Fax: (514) 398-7857. E-mail: greg_matlashewski{at}maclan.mcgill.ca.

Molecular and Cellular Biology, February 1999, p. 1092-1100, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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