Modification of DNA radiolysis by DNA-binding proteins: structural aspects.


Formation of specific complexes between proteins and their cognate DNA modulates the yields and the location of radiation damage on both partners of the complex. The radiolysis of DNA-protein complexes is studied for: (1) the Escherichia coli lactose operator-repressor complex, (2) the complex between DNA bearing an analogue of an abasic site and the repair protein Fpg of Lactococcus lactis. Experimental patterns of DNA damages are presented and compared to predicted damage distribution obtained using an improved version of the stochastic model RADACK. The same method is used for predicting the location of damages on the proteins. At doses lower than a threshold that depends on the system, proteins protect their specific binding site on DNA while at high doses, the studied complexes are disrupted mainly through protein damage. The loss of binding ability is the functional consequence of the amino-acids modification by OH* radicals. Many of the most probably damaged amino acids are essential for the DNA-protein interaction and within a complex are protected by DNA.

Cite this paper

@article{Davidkova2006ModificationOD, title={Modification of DNA radiolysis by DNA-binding proteins: structural aspects.}, author={M. Davidkova and Viktorie St{\'i}sov{\'a} and St{\'e}phane Goffinont and Nathalie Gillard and Bertrand Castaing and M{\'e}lanie Spotheim-Maurizot}, journal={Radiation protection dosimetry}, year={2006}, volume={122 1-4}, pages={100-5} }