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

Paula N. Friedman, Xinbin Chen, Jill Bargonetti, Carol Prives

Research output: Contribution to journalArticle

193 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)3319-3323
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number8
StatePublished - Apr 15 1993
Externally publishedYes

Fingerprint

Southwestern Blotting
DNA
Viral DNA
Centrifugation
Gel Chromatography
Sucrose
Proteins
Gels
Ligands

Keywords

  • Chemical crosslinking
  • DNA-binding protein
  • Gel filtration
  • Sucrose gradients
  • Tumor suppressor

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

The p53 protein is an unusually shaped tetramer that binds directly to DNA. / Friedman, Paula N.; Chen, Xinbin; Bargonetti, Jill; Prives, Carol.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, No. 8, 15.04.1993, p. 3319-3323.

Research output: Contribution to journalArticle

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