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. 1993 Apr 15;90(8):3319–3323. doi: 10.1073/pnas.90.8.3319

The p53 protein is an unusually shaped tetramer that binds directly to DNA.

P N Friedman 1, X Chen 1, J Bargonetti 1, C Prives 1
PMCID: PMC46291  PMID: 8475074

Abstract

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.

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Selected References

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