The DNA binding domain of the human c-Abl tyrosine kinase preferentially binds to DNA sequences containing an AAC motif and to distorted DNA structures

Biochemistry
M H David-CordonnierJ C D'Halluin

Abstract

The c-Abl tyrosine kinase protein is implicated in the signaling pathway as well as in transcription, DNA repair, apoptosis, and several other vital biological processes essential for cell proliferation or differentiation. The interaction of c-Abl with DNA is important for some of these functions, but the exact nature of this interaction is still a matter of controversy. The present study addresses the DNA-binding properties of the human c-Abl protein. Using CASTing experiments, the consensus binding site 5'-AA/CAACAAA/C was determined. The central highly conserved AAC triplet appears to constitute the crucial core element in the binding sequences of the c-Abl protein. The c-Abl DNA-binding domain recognizes specific sequences and interacts with deformed DNA structures such as four-way junctions and bubble DNA containing a large single-stranded loop, as determined by electromobility shift assay, melting temperature studies, and binding to specific oligonucleotides covalently linked to beads. Additional competition experiments suggest that the interaction mainly involves contacts within the minor groove of the double helix. The DNA-binding properties of c-Abl are reminiscent of those of high-mobility group (HMG)-like proteins su...Continue Reading

References

Jan 1, 1991·Annual Review of Biochemistry·R A Young

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Citations

Jul 9, 1999·Biochimica Et Biophysica Acta·M H David-CordonnierJ C D'Halluin
Jul 26, 2011·Molecular Cancer·Zhihua JiangBaskaran Rajasekaran
Feb 5, 2008·Journal of Virological Methods·Ana Carolina Magalhães Andrade de GóesJosé Paulo Gagliardi Leite
Aug 21, 2010·Journal of Nucleic Acids·Gaëlle Lenglet, Marie-Hélène David-Cordonnier
Mar 14, 2000·Cell Death and Differentiation·Y Shaul
Sep 28, 2004·The Journal of Biological Chemistry·Donghui YuAjit Bharti
May 31, 2003·Journal of Cell Science·Pamela J WoodringJean Y J Wang

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