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

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

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	3319-3323
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	90
Issue number	8
State	Published - Apr 15 1993
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

General
Genetics

Cite this

@article{21aab30f877d4967846981b37a1be024,

title = "The p53 protein is an unusually shaped tetramer that binds directly to DNA",

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.",

keywords = "Chemical crosslinking, DNA-binding protein, Gel filtration, Sucrose gradients, Tumor suppressor",

author = "Friedman, {Paula N.} and Xinbin Chen and Jill Bargonetti and Carol Prives",

year = "1993",

month = apr,

day = "15",

language = "English (US)",

volume = "90",

pages = "3319--3323",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "8",

}

TY - JOUR

T1 - The p53 protein is an unusually shaped tetramer that binds directly to DNA

AU - Friedman, Paula N.

AU - Chen, Xinbin

AU - Bargonetti, Jill

AU - Prives, Carol

PY - 1993/4/15

Y1 - 1993/4/15

N2 - 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.

AB - 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.

KW - Chemical crosslinking

KW - DNA-binding protein

KW - Gel filtration

KW - Sucrose gradients

KW - Tumor suppressor

UR - http://www.scopus.com/inward/record.url?scp=0027522365&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027522365&partnerID=8YFLogxK

M3 - Article

C2 - 8475074

AN - SCOPUS:0027522365

VL - 90

SP - 3319

EP - 3323

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 8

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Other files and links

Fingerprint

Cite this