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J. Biol. Chem., Vol. 275, Issue 45, 35040-35050, November 10, 2000

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Equilibrium and Kinetic Binding Interactions between DNA and a Group of Novel, Nonspecific DNA-binding Proteins from Spores of Bacillus and Clostridium Species^*

Christopher S. Hayes, Zheng-Yu Peng, and Peter Setlow^§

From the Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030

Binding of /-type small acid-soluble spore proteins (SASP) is the major determinant of DNA resistance to damage caused by UV radiation, heat, and oxidizing agents in spores of Bacillus and Clostridium species. Analysis of several /-type SASP showed that these proteins have essentially no secondary structure in the absence of DNA, but become significantly -helical upon binding to double-stranded DNAs or oligonucleotides. Folding of /-type SASP induced by a variety of DNAs and oligonucleotides was measured by CD spectroscopy, and this allowed determination of a DNA binding site size of 4 base pairs as well as equilibrium binding parameters of the /-type SASP-DNA interaction. Analysis of the equilibrium binding data further allowed determination of both intrinsic binding constants (K) and cooperativity factors (), as the /-type SASP-DNA interaction was significantly cooperative, with the degree of cooperativity depending on both the bound DNA and the salt concentration. Kinetic analysis of the interaction of one /-type SASP, SspC^Tyr, with DNA indicated that each binding event involves the dimerization of SspC^Tyr monomers at a DNA binding site. The implications of these findings for the structure of the /-type SASP·DNA complex and the physiology of /-type SASP degradation during spore germination are discussed.

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