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How cells recognize damaged DNA: clues from xeroderma pigmentosum and yeast
1Department of Medicine, Stanford University School of Medicine, CA 94305.
Progress in Clinical and Biological Research
|January 1, 1990
Summary
Researchers found a DNA repair factor missing in Xeroderma pigmentosum (XP) group E. This XPE binding factor is elevated in cisplatin-resistant tumors and may be the human photolyase homolog.
Area of Science:
- Molecular Biology
- Genetics
- DNA Repair Mechanisms
Background:
- Xeroderma pigmentosum (XP) involves defective DNA excision repair of UV and cisplatin damage.
- XP complementation group E is characterized by a specific DNA repair defect.
Purpose of the Study:
- Identify a DNA damage recognition factor in human cells.
- Investigate the role of this factor in XP and cisplatin resistance.
- Determine if this factor is the human homolog of photolyase.
Main Methods:
- Human cell analysis
- DNA damage recognition assays
- Gene expression analysis in tumor cell lines
Main Results:
- A novel factor, XPE binding factor, was identified in human cells.
- This factor recognizes multiple DNA damage types and is absent in XP group E.
- XPE binding factor levels are five-fold higher in cisplatin-resistant tumor cells.
- The factor shares binding characteristics with yeast photolyase but lacks photoreactivating activity.
Conclusions:
- XPE binding factor plays a role in DNA repair and may be linked to cisplatin resistance.
- The findings suggest XPE binding factor is the human homolog of photolyase.