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Science 10 January 1992:
Vol. 255. no. 5041, pp. 203 - 206
DOI: 10.1126/science.1553548
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Articles

Science, Vol 255, Issue 5041, 203-206
Copyright © 1992 by American Association for the Advancement of Science

articles

Dimerization of a specific DNA-binding protein on the DNA

B Kim and JW Little

Department of Biochemistry, University of Arizona, Tucson 85721.

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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