The BCR-ABL Oncoprotein Potentially Interacts with the Xeroderma Pigmentosum Group B Protein
Abstract
The previously uncharacterized CDC24 homology domain of BCR, which is missing in the P185 BCR-ABL oncogene of Philadelphia chromosome (Ph1)-positive acute lymphocytic leukemia but is retained in P210 BCR-ABL of chronic myelogeneous leukemia, was found to bind to the xeroderma pigmentosum group B protein (XPB). The binding appeared to be required for XPB to be tyrosine-phosphorylated by BCR-ABL. The interaction not only reduced both the ATPase and the helicase activities of XPB purified in the baculovirus system but also impaired XPB-mediated cross-complementation of the repair deficiency in rodent UV-sensitive mutants of group 3. The persistent dysfunction of XPB may in part underlie genomic instability in blastic crisis.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- January 1999
- DOI:
- 10.1073/pnas.96.1.203
- Bibcode:
- 1999PNAS...96..203T