Determination of the human c-Abl consensus DNA binding site
Identifieur interne : 000278 ( France/Analysis ); précédent : 000277; suivant : 000279Determination of the human c-Abl consensus DNA binding site
Auteurs : Marie-Hélène David-Cordonnier [France] ; Malika Hamdane [France] ; Christian Bailly [France] ; Jean-Claude D'Halluin [France]Source :
- FEBS Letters [ 0014-5793 ] ; 1998.
English descriptors
- Teeft :
- Actin binding site, Anking sequences, Base pairs, Binding activity, Binding capacity, Binding domain, Binding sites, Bold letters, Cell cycle, Clone, Computer programs, Consensus binding site, Consensus sequence, Deletion, Deletion mutants, Dnase, Domain, Feb, Fusion peptide, Fusion protein, Human protein, Kinase, Klenow enzyme, Large domain, Ligue nationale contre, Lille, Mouse protein, Mutant, Protein binding site, Secondary structure, Target site, Threonine residues, Tyrosine, Tyrosine kinase, Wang.
Abstract
Abstract: 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′-AA/CAACAAA/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.
Url:
DOI: 10.1016/S0014-5793(98)00169-0
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: 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′-AA/CAACAAA/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.</div>
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