Dissociation constant of GAGA transcription factor from DNA

Value 5.2 nM
Organism Fruit fly Drosophila melanogaster
Reference Nalefski EA, Nebelitsky E, Lloyd JA, Gullans SR. Single-molecule detection of transcription factor binding to DNA in real time: specificity, equilibrium, and kinetic parameters. Biochemistry. 2006 Nov 21 45(46):13794-806 Table - link PubMed ID17105198
Primary Source Pedone PV et al, The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding, Proc Natl Acad Sci U S A. 1996 Apr 293(7):2822-6PubMed ID8610125
Method Result from Electrophoretic Mobility Shift Assay (EMSA) using isolated GAGA factor ZFD in intermediate ionic strength buffer. EMSA is a shift assay technique which can determine DNA-protein or RNA protein interactions and association/dissociation kinetics. A nucleic acid-protein complex is run in gel next to a control lane that has only nucleic acid. The complex moves slower due to higher mass. Known starting nucleic acid and protein concentrations enable determination of affinity.
Entered by Uri M
ID 104594