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Science 17 April 1992:
Vol. 256. no. 5055, pp. 382 - 385
DOI: 10.1126/science.256.5055.382
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Articles

Cell Cycle—Regulated Binding of c-Abl Tyrosine Kinase to DNA

Edward T. Kipreos 1 and Jean Y. J. Wang 1

1 Department of Biology and Center for Molecular Genetics, University of California San Diego, La Jolla, CA 92093-0116

The proto-oncogene c-abl encodes a protein tyrosine kinase that is localized in the cytoplasm and the nucleus. The large carboxyl-terminal segment of c-Abl was found to contain a DNA-binding domain that was necessary for the association of c-Abl with chromatin. The DNA-binding activity of c-Abl was lost during mitosis when the carboxyl-terminal segment became phosphorylated. In vitro phosphorylation of the DNA-binding domain by cdc2 kinase abolished DNA binding. Homozygous mutant mice expressing a c-Abl tyrosine kinase without the DNA-binding domain have been reported to die of multiple defects at birth. Thus, binding of the c-Abl tyrosine kinase to DNA may be essential to its biological function.


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