Analysis of Specific Protein-DNA Interactions
The central issue in the regulation of genome functions is the mechanism of sequence-specific protein-nucleic acid interactions. Gene expression, replication, recombination and DNA condensation in chromatin are steered by binding of regulatory protein ligands to specific sites in DNA. Numerous methods have been developed to study protein-DNA interactions. In this chapter we discuss two widely used and straightforward approaches to address this problem.
KeywordsGlycerol Phenol EDTA Recombination Ampicillin
Unable to display preview. Download preview PDF.
- Carey J (1991) Gel retardation. In: Sauer RT (ed) Protein-DNA Interactions. Methods Enzymol. vol 208. Academic Press, London, pp 103–117Google Scholar
- Lizzaraga B, Sanchez-Romero D, Gil A, Melgar E (1978) The role of Ca2+ on pH-induced hydrodynamic changes of bovine pancreatic deoxyribonuclease A. J Biol Chem 253: 3191–3195Google Scholar
- Maxam AM, Gilbert W (1980) Sequencing end-labelled DNA with base-specific chemical cleavages. In: Grossman L, Moldave K (eds) Nucleic acids. Methods Enzymol, vol 65. Academic Press, London, pp 499–599Google Scholar
- Pedersen H, Sogaard-Andersen L, Holst B, Gerlach P, Bremer E, Valentin-Hansen P (1992) cAMP-CRP activator complex and the CytR repressor protein bind co-operatively to the cytRP promoter in Escherichia coli and CytR antagonizes the cAMP-CRP-induced DNA bend. J Mol Biol 227: 396–406PubMedCrossRefGoogle Scholar
- Sambrook J, Fritch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, New YorkGoogle Scholar