Open AccessThe p53 protein is an unusually shaped tetramer that binds directly to DNA.
Author(s) -
Paula N. Friedman,
Xinbin Chen,
Jill Bargonetti,
Carol Prives
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.8.3319
Subject(s) - tetramer , dna , size exclusion chromatography , chemistry , sucrose gradient , monomer , centrifugation , microbiology and biotechnology , blot , biochemistry , biophysics , biology , gene , membrane , organic chemistry , enzyme , polymer
We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA.