THE P53 PROTEIN IS AN UNUSUALLY SHAPED TETRAMER THAT BINDS DIRECTLY TO DNA

被引：244

作者：

FRIEDMAN, PN ^{[1
]}

CHEN, XB ^{[1
]}

BARGONETTI, J ^{[1
]}

PRIVES, C ^{[1
]}

机构：

[1] COLUMBIA UNIV, DEPT BIOL SCI, NEW YORK, NY 10027 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 08期

关键词：

TUMOR SUPPRESSOR; CHEMICAL CROSS-LINKING; GEL FILTRATION; SUCROSE GRADIENTS; DNA-BINDING PROTEIN;

D O I：

10.1073/pnas.90.8.3319

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：3319 / 3323

页数：5

共 31 条

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ADDISON C, 1990, ONCOGENE, V5, P423

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