UV damage-specific DNA-binding protein in xeroderma pigmentosum complementation group E.
The gel mobility shift assay method revealed a specifically ultraviolet (UV) damage recognizing, DNA-binding protein in nuclear extracts of normal human cells. The resulted DNA/protein complexes caused the two retarded mobility shifts. Four xeroderma pigmentosum complementation group E (XPE) fibroblast strains derived from unrelated Japanese families were not deficient in such a DNA damage recognition/binding protein because of the normal complex formation and gel mobility shifts, although we confirmed the reported lack of the protein in the European XPE (XP2RO and XP3RO) cells. Thus, the absence of this binding protein is not always commonly observed in all the XPE strains, and the partially repair-deficient and intermediately UV-hypersensitive phenotype of XPE cells are much similar whether or not they lack the protein.
Kataoka
H
H
Department of Radiation Biophysics, Kobe University School of Medicine, Japan.
Fujiwara
Y
Y
D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D004249:DNA Damage; D015342:DNA Probes; D004268:DNA-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D005347:Fibroblasts; D005816:Genetic Complementation Test; D006801:Humans; D015345:Oligonucleotide Probes; D012867:Skin; D014466:Ultraviolet Rays; D014983:Xeroderma Pigmentosum / Q000235:genetics*
D015342:DNA Probes; D004268:DNA-Binding Proteins; D015345:Oligonucleotide Probes