Analysis of a protein-binding domain of p53

Ruppert, J. M., Stillman, B. (1993) Analysis of a protein-binding domain of p53. Mol Cell Biol, 13 (6). pp. 3811-20. ISSN 0270-7306 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8388547
DOI: 10.1128/MCB.13.6.3811

Abstract

The tumor suppressor protein p53 was first isolated as a simian virus 40 large T antigen-associated protein and subsequently was found to function in cell proliferation control. Tumor-derived mutations in p53 occur predominantly in four evolutionarily conserved regions spanning approximately 50% of the polypeptide. Previously, three of these regions were identified as essential for T-antigen binding. We have examined the interaction between p53 and T antigen by using Escherichia coli-expressed human p53. By a combination of deletion analysis and antibody inhibition studies, a region of p53 that is both necessary and sufficient for binding to T antigen has been localized. This function is contained within residues 94 to 293, which include the four conserved regions affected by mutation in tumors. Residues 94 to 293 of p53 were expressed in both wild-type and mutant forms. T-antigen binding was unaffected by tumor-derived mutations which have been associated with the wild-type conformation of p53 but was greatly reduced by mutations which were previously shown to alter p53 conformation. Our results show that, like T-antigen binding to the Rb tumor suppressor protein, T antigen appears to interact with the domain of p53 that is commonly mutated in human tumors.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Antigens Polyomavirus Transforming metabolism Base Sequence Binding Sites Cell Line Cell Nucleus/metabolism Escherichia coli genetics Glutathione Transferase genetics metabolism Humans Molecular Sequence Data Mutagenesis Oligodeoxyribonucleotides Protein Conformation Recombinant Fusion Proteins metabolism Simian virus 40 genetics Transfection Tumor Suppressor Protein p53 genetics metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > p53
CSHL Authors:
Communities: CSHL labs > Stillman lab
Highlight: Stillman, Bruce W.
Depositing User: CSHL Librarian
Date Deposited: 02 Mar 2012 18:46
Last Modified: 20 Jun 2017 19:57
PMCID: PMC359868
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25048

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