Dimerization of a Specific DNA-Binding Protein on the DNA
- 10 January 1992
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 255 (5041) , 203-206
- https://doi.org/10.1126/science.1553548
Abstract
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.Keywords
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