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Determination of the human c‐Abl consensus DNA binding site
Author(s) -
David-Cordonnier Marie-Hélène,
Hamdane Malika,
Bailly Christian,
D'Halluin Jean-Claude
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00169-0
Subject(s) - biology , dna binding site , footprinting , microbiology and biotechnology , dna , binding site , hmg box , abl , dna binding domain , fusion protein , genetics , tyrosine kinase , dna binding protein , transcription factor , signal transduction , promoter , gene , gene expression , recombinant dna , base sequence
c‐Abl tyrosine kinase, an essential protein of the cell cycle signalling pathways, is implicated in the regulation of RNA polymerase II activity, apoptosis and DNA repair. Its DNA binding activity is important for its biological functions. However, the molecular basis of c‐Abl interaction with DNA remains largely unclear. We delimited the human c‐Abl DNA binding domain and identified its preferred binding site, 5′‐A A / C AACAA A / C . The central AAC motif is highly conserved and constitutes the major core element in the binding sites. EMSAs and footprinting experiments were performed to explore how the c‐Abl fusion protein recognizes specific sequences in DNA.