Biophysical analysis of the interaction of toxic metal ions and oxidants with the zinc finger domain of XPA.
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.
Hartwig
Andrea
A
Fachgebiet Lebensmittelchemie und Toxikologie, Technische Universität Berlin, Berlin, Germany.
Schwerdtle
Tanja
T
Bal
Wojciech
W
D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008670:Metals / Q000737:chemistry* / Q000378:metabolism*; D016877:Oxidants / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D021241:Spectrometry, Mass, Electrospray Ionization; D051760:Xeroderma Pigmentosum Group A Protein / Q000737:chemistry* / Q000378:metabolism*; D015032:Zinc / Q000737:chemistry / Q000378:metabolism; D016335:Zinc Fingers / Q000235:genetics*
D008670:Metals; D016877:Oxidants; D051760:Xeroderma Pigmentosum Group A Protein; D015032:Zinc