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.
MeSH terms
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Adenosine Triphosphatases / analysis
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Animals
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Blast Crisis / etiology*
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CHO Cells
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Cell Cycle Proteins / metabolism*
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Cricetinae
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DNA Helicases / analysis
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DNA-Binding Proteins / metabolism*
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Dose-Response Relationship, Radiation
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Fusion Proteins, bcr-abl / metabolism*
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Guanine Nucleotide Exchange Factors*
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Humans
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Leukemia, Myelogenous, Chronic, BCR-ABL Positive / genetics*
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Protein Binding
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Proto-Oncogene Proteins / metabolism*
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Ultraviolet Rays
Substances
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CDC24 protein, S cerevisiae
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Cell Cycle Proteins
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DNA-Binding Proteins
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Guanine Nucleotide Exchange Factors
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Proto-Oncogene Proteins
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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XPBC-ERCC-3 protein
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Fusion Proteins, bcr-abl
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Adenosine Triphosphatases
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DNA Helicases