Abstract
Zinc-binding domains are frequently present in proteins required for maintaining genomic integrity. During recent years there has been accumulating evidence that they may be particularly sensitive targets for toxic metal ions, leading, for example, to DNA repair inhibition. Here, we present a broad set of methods for assessing the impact of metal ions on the zinc-binding domain of xeroderma group A protein, an essential factor in nucleotide excision repair. We envisage that these methods will be useful also for other proteins.
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Acknowledgments
This research was supported by the Deutsche Forschungsgemeinschaft, grants no. HA 2372/3-4, SCHW 903/3-2, and by the Alexander von Humboldt-Stiftung subsistence grant to WB.
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Hartwig, A., Schwerdtle, T., Bal, W. (2010). Biophysical Analysis of the Interaction of Toxic Metal Ions and Oxidants with the Zinc Finger Domain of XPA. In: Mackay, J., Segal, D. (eds) Engineered Zinc Finger Proteins. Methods in Molecular Biology, vol 649. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-753-2_25
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DOI: https://doi.org/10.1007/978-1-60761-753-2_25
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