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A more recent version of this article appeared on December 20, 2002
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Papers In Press, published online ahead of print October 11, 2002
J. Biol. Chem, 10.1074/jbc.M208540200
Submitted on August 20, 2002
Revised on October 5, 2002
Accepted on October 11, 2002

Role of Hydration in the Binding of Lac Repressor to DNA

Michael G. Fried, Douglas F. Stickle, Karen V. Smirnakis, Claire Adams, Douglas MacDonald, and Ponzy Lu

Biochemistry and Molecular Biology, The Penn State University College of Medicine, Hershey, PA 17033

Corresponding Author: mfried{at}psu.edu

The osmotic stress technique was used to measure changes in macromolecular hydration that accompany binding of wild-type E. coli lactose (lac) repressor to its regulatory site (operator O1) in the lac promoter, and its transfer from site O1 to nonspecific DNA. Binding at O1 is accompanied by the net release of 260 ± 32 water molecules. If all are released from macromolecular surfaces, this result is consistent with a net reduction of solvent-accessible surface area of 2370 ± 550Å2. This area is only slightly smaller than the macromolecular interface calculated for a crystalline repressor dimer-O1 complex, but is significantly smaller than that for the corresponding complex with the symmetrical optimized Osym operator. The transfer of repressor from site O1 to nonspecific DNA is accompanied by the net uptake of 93 ± 10 water molecules. Together these results imply that formation of a nonspecific complex is accompanied by the net release of 165 ± 43 water molecules. The enhanced stabilities of repressor-DNA complexes with increasing osmolality may contribute to the ability of E. coli cells to tolerate dehydration and/or high external salt concentrations.


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