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

被引:241
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
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
收藏
页码:3319 / 3323
页数:5
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