alexa The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein.
Nursing

Nursing

Advanced Practices in Nursing

Author(s): Takeda N, Shibuya M, Maru Y, Takeda N, Shibuya M, Maru Y

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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.
This article was published in Proc Natl Acad Sci U S A and referenced in Advanced Practices in Nursing

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