Abstract
The Escherichia coli protein, RecA, is critical for maintaining genetic integrity. RecA catalyzes DNA pairing and strand exchange reactions that are utilized in DNA recombination and DNA repair. Buffer and salt conditions influence the aggregation and activity of RecA. In low salt conditions, RecA is a DNA-dependent ATPase. However, prior research demonstrated that high salt concentrations allow RecA to hydrolyze ATP in the absence of DNA and at levels comparable to those obtained in the presence of DNA [Pugh, B. F. and Cox, M. M. (1988) Journal of Biological Chemistry 263, 76-83]. We have used circular dichroism (CD) and fluorescence spectroscopies to better understand the salt-induced effects on RecA structure and function. CD and fluorescence studies were performed in order to monitor the thermally induced unfolding of RecA in the presence of a variety of salts. We found that different salts had unique effects on RecA unfolding transitions and stability. Unfolding studies performed under salt conditions known to activate RecA's ATPase activity showed unique, thermally stable RecA structures. A comparison of the influences of different ions on RecA unfolding will be presented. These studies may help to elucidate how different ions influence RecA activity, structure, aggregation, and stability.
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