DIMERIZATION OF A SPECIFIC DNA-BINDING PROTEIN ON THE DNA

被引:127
作者
KIM, B [1 ]
LITTLE, JW [1 ]
机构
[1] UNIV ARIZONA,DEPT MOLEC & CELLULAR BIOL,TUCSON,AZ 85721
关键词
D O I
10.1126/science.1553548
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
Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.
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页码:203 / 206
页数:4
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