The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein.
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.
Mesh Terms:
Adenosine Triphosphatases, Animals, Blast Crisis, CHO Cells, Cell Cycle Proteins, Cricetinae, DNA Helicases, DNA-Binding Proteins, Dose-Response Relationship, Radiation, Fusion Proteins, bcr-abl, Guanine Nucleotide Exchange Factors, Humans, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Protein Binding, Proto-Oncogene Proteins, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Ultraviolet Rays
Adenosine Triphosphatases, Animals, Blast Crisis, CHO Cells, Cell Cycle Proteins, Cricetinae, DNA Helicases, DNA-Binding Proteins, Dose-Response Relationship, Radiation, Fusion Proteins, bcr-abl, Guanine Nucleotide Exchange Factors, Humans, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Protein Binding, Proto-Oncogene Proteins, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Ultraviolet Rays
Proc. Natl. Acad. Sci. U.S.A.
Date: Jan. 05, 1999
PubMed ID: 9874796
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