Abstract
1,10-Phenanthroline-copper ion is an efficient chemical nuclease which makes single-stranded nicks in DNA at physiological pH’s and temperatures. In addition to serving as a reliable footprinting reagent, it is useful for defining functionally important sequence-dependent conformational variability of DNA and protein-induced structural changes in DNA.
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References
Cartwright IL, Elgin S (1982) Analysis of chromatin structure and DNA sequence organization: use of 1,10-phenanthroline-cuprous complex. NAR 10: 5835–5851
Chen C-H B, Sigman DS (1986) Nuclease activity of 1,10-phenanthroline-copper. Sequence-specific targeting. Proc Natl Acad Sci USA 83: 7147–7151
Chen C-H B. Sigman DS (1987) Chemical conversion of a DNA-binding protein into a site-specific nuclease. Science 237: 1197–1201
Crothers DM (1987) Gel electrophoresis of protein-DNA complexes. Nature 325: 464–465
D’Aurora V, Stem AM, Sigman DS (1977) Inhibition of E. coliDNA polymerase I by 1,10-phenanthroline. Biochem Biophys Res Commun 78: 170–176
D’Aurora V, Stern AM, Sigman DS (1978) 1,10-Phenanthroline-cuprous ion complex, a potent inhibitor of DNA and RNA polymerases. Biochem Biophys Res Commun 80:1025–1032
de Crombnigghe B, Busby S, Buc H. (1984) Cyclic AMP receptor protein: role in transcription activation. Science 224: 831–837
Drew HR, Travers AA (1984) DNA structural variations in the E. colityr T promoter. Cell 37: 491–502
Galas DJ, Schmitz A (1978) DNAse footprinting, a simple method for the detection of protein-DNA binding specificity. NAR 5: 3157–3170
Goyne TE, Sigman DS (1987) Nuclease activity of 1,10-phenanthroline-copper ion. Chemistry of deoxyribose oxidation. J Am Chem Soc 109: 2846–2848
Graham DR, Sigman DS (1984) Zinc ion in E. coliDNA polymerase L A reinvestigation. Inorg Chem 23: 4188–4191
Groves JT, Subramanian DV (1984) Hydroxylation by cytochrome P-450 and metalloporphyrin models. Evidence for allylic rearrangement. J Am Chem Soc 106: 2177–2181
Jessee B, Gargiulo G, Razvi F, Worcel A (1982) Analgous cleavage of DNA by micrococcal nuclease and 1,10-phenanthroline-cuprous complex. NAR 10: 5823–5834
Kirkegaard K, Buc H, Spassky A, Wang J (1983) Mapping of single-stranded regions in duplex DNA at the sequence level: single-strand specific cytosine methylation in RNA polymerase-promoter complexes. Proc Natl Acad Sci USA 80: 2544–2548
Kuwabara MD, Sigman DS (1987) Footprinting DNA-protein complexes in situ following gel retardation assays using 1,10-phenanthroline-copper ion: Escherichia coliRNA polymerase-lac promoter complexes. Biochemistry 26: 7234–7238
Kuwabara M, Yoon C, Goyne TE, Thederahn T, Sigman DS (1986) Nuclease activity of 1,10-phenanthroline-copper ion and its complexes with netropsin and EcoRI. Biochemistry 25: 7401–7408
Marshall LE, Graham DR, Reich KA, Sigman DS (1981) Cleavage of DNA by the 1,10-phenanthroline-cuprous complex. Hydrogen peroxide requirement: primary and secondary structure specificity. Biochemistry 20: 244–250
Pope LE, Sigman DS (1984) Secondary structure specifity of the nuclease activity of 1,10-phenanthroline-copper complex. Proc Natl Acad Sci 81: 3–7
Pope LM, Reich KA, Graham DR, Sigman DS (1982) Products of DNA cleavage by the 1,10-phenanthroline copper complex. Identification of E. coliDNA polymerase I inhibitors. J Biol Chem 257: 12121–12128
Pribnow D (1975) Nucleotide sequence of an RNA polymerase binding site at an early T7 promoter. Proc Natl Acad Sci USA 72: 784–788
Revzin A, Geglarek M, Garner M (1986) Comparison of nucleic acid-protein interactions in solution and in polyacrylamide gels. Anal Biochem 153: 172–177
Scheffler LE, Elson EL, Baldwin RL (1968) Helix formation by dAT oligomers. I. Hairpin and straight-chain helices. J Mol Biol 36: 291–304
Sigman DS, Graham DR, D’Aurora V, Stem AM (1979) Oxygen-dependent cleavage of DNA by the 1,10-phenanthroline-cuprous complex. Inhibition of E. coliDNA polymerase I. J Biol Chem 254: 12269–12272
Sigman DS, Spassky A, Rimsky S, Buc H (1985) Conformational analysis of lac promoters using the nuclease activity of 1,10-phenanthroline-copper ion. Biopolymers 24: 183–197
Slater JP, Mildvan AS, Loeb LA (1971) Zinc in DNA polymerases. Biochem Biophys Res Commun 44: 37–43
Spassky A (1986) Visualization of the movement of the Escherichia coliRNA polymerase along the lac UV5 promoter during the initiation of the transcription. J Mol Biol 188: 99–103
Spassky A, Sigman DS (1985) Nuclease activity of 1,10-phenanthroline-copper ion. Conformational analysis and footprinting of the lac operon. Biochemistry 24: 8050–8056
Spassky A, Sigman DS (1985) Nuclease activity of 1,10-phenanthroline-copper ion. Conformational analysis and footprinting of the lac operon. Biochemistry 24: 8050–8056
Springgate CF, Mildvan AS, Abramson R, Engle JL, Loeb LA (1973) Escherichia coli deoxyribonucleic acid polymerase I, a zinc metalloenzyme. J Biol Chem 248:5987–5993
Thederahn T, Sigman DS (1988) Nuclease activity of 1,10-phenanthroline-copper. Kinetic mechanism. J Am Chem Soc (in press)
Yoon C, Kuwabara M, Law R, Wall R, Sigman DS (1988) Sequence-dependent variability of DNA structure. J Biol Chem 263: 8458–8643
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© 1989 Springer-Verlag Berlin Heidelberg
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Sigman, D.S., Spassky, A. (1989). DNase Activity of 1,10-Phenanthroline-Copper Ion. In: Eckstein, F., Lilley, D.M.J. (eds) Nucleic Acids and Molecular Biology. Nucleic Acids and Molecular Biology, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-83709-8_2
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DOI: https://doi.org/10.1007/978-3-642-83709-8_2
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