Abstract
We have previously reported a cisplatin-selected HeLa cell line showing cross-resistance to ultraviolet (UV) radiation and overexpression of UV-damage recognition factors (Chao et al., Mol. Cell. Biol., 11, 2075-2080, 1991). Here, we further characterize a UV-damage recognition factor in vitro using a gel mobility shift assay. The results indicate that the damage-recognition factor is (i) localized mostly in the nucleus, (ii) protease-sensitive, (iii) RNA-independent, (iv) active in a wide range of ionic strengths (50-400 mM NaCl), (v) with a high affinity for UV-damaged DNA (50-fold molar excess competitor causes 50% recognition loss), and (vi) resistant to agents and that modify protein conformation (urea and NP-40), but slightly sensitive to CaCl2. The significance of the identified UV-damage recognition factor in the sensitivity or resistance of cells to UV is also discussed.
| Original language | American English |
|---|---|
| Pages (from-to) | 105-113 |
| Journal | Mutation research |
| Volume | 281 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1992 |
Keywords
- Chloramphenicol O-Acetyltransferase/metabolism
- Cisplatin/pharmacology
- DNA Damage/genetics
- DNA Repair/genetics
- DNA-Binding Proteins/drug effects
- DNA-Binding Proteins/metabolism
- DNA/radiation effects
- Electric Stimulation
- HeLa Cells/radiation effects
- Humans
- Nuclear Proteins/drug effects
- Nuclear Proteins/metabolism
- Plasmids/genetics
- Protein Conformation/drug effects
- Ultraviolet Rays