c-Abl tyrosine kinase, an essential protein of the cell cycle signalli
ng pathways, is implicated in the regulation of RNA polymerase II acti
vity, apoptosis and DNA repair. Its DNA binding activity is important
for its biological functions. However, the molecular basis of c-Abl in
teraction with DNA remains largely unclear. We delimited the human c-A
bl DNA binding domain and identified its preferred binding site, 5'-A(
A)/(C)AACAA(A)/(C). The central AAC motif is highly conserved and cons
titutes the major core element in the binding sites. EMSAs and footpri
nting experiments were performed to explore how the c-Abl fusion prote
in recognizes specific sequences in DNA. (C) 1998 Federation of Europe
an Biochemical Societies.