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 |
Fingerprint
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 journal › Article
}
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 -