Nuclease activity of 1,10-phenanthroline-copper ion. Chemistry of deoxyribose oxidation

Goyne, Thomas; Sigman, David S.

doi:10.1021/ja00243a060

Cited by 152 publications

(120 citation statements)

References 1 publication

Supporting

Mentioning

113

Contrasting

Unclassified

Order By: Relevance

“…These sites were predicted to allow the close approach of the OP moiety to the C-1 H of one or more deoxyriboses. The C-1 H of the deoxyribose is most likely the principal site of oxidative attack by the Fis-OP chimeras because it is the reactive position in DNA cleavage by the free 2:1 complex of OP-Cu+ (18). An alternative site of attack is the CA4 H, but oxidation at that position would generate 3'-phosphoglycolates, not 3'-phosphomonoesters, and there is no evidence for the formation of this product by gel electrophoresis (Fig.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Structure of the Escherichia coli Fis-DNA complexprobed by protein conjugated with 1,10-phenanthroline copper(I)complex.

Pan

Feng

Finkel

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The Escherichia coi Fis (factor for inversion stimulation) protein functions in many diverse biological systems including recombination, transcription, and DNA replication. Although Fis is a site-specific DNA-binding protein, it lacks a well-defined consensus recognition sequence. The electrophoretic mobility of Fis-DNA complexes, along with considerations ofthe Fis crystal structure, indicates that significant deformation of DNA occurs upon Fis binding. The factor for inversion stimulation (Fis) is a small basic protein in Escherichia coli that was initially identified because of its role in stimulating site-specific DNA inversion by the Hin and Gin recombinases. In this role, Fis binds sitespecifically to a recombinational enhancer that becomes associated with the two recombination sites in a complex nucleoprotein structure. Fis has also been shown to function in phage A site-specific recombination, transcriptional activation of rRNA and tRNA operons, repression of its own synthesis, and oriC-directed DNA replication (1). The x-ray crystal structure ofFis (2, 3) reveals it to be a homodimer with each 98-amino acid monomer containing four a-helices (Fig. 1) ices (D and D') are positioned only 25 A from each other, which is too short a distance to insert into adjacent major grooves of straight B-DNA. In the absence of a Fis-DNA cocrystal structure, nuclease and chemical footprinting combined with mutation data were used to construct a model of Fis bound to the distal site of the Hin gene (hin) enhancer that contains a DNA bending angle of , =60°(3, 8 §To whom reprint requests should be sent at t address. 1721The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

show abstract

Section: Discussionmentioning

confidence: 99%

“…Substitution of these side chains with an OP on an acetamido segment linked to a ysteine ( Fig. 1) has the potential to approach a C-1 H atom of a deoxyribose from the minor groove, the target of attack by the free OP-Cu complex (18).…”

Section: Methodsmentioning

confidence: 99%

Structure of the Escherichia coli Fis-DNA complexprobed by protein conjugated with 1,10-phenanthroline copper(I)complex.

Pan

Feng

Finkel

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Oxidation of DNA deoxyribose at the C1′ position plays an important role in the chemistry of DNA damage by a variety of agents, such as (1,10-phenanthroline) copper complex [(OP) 2 Cu] (1-8), enediyne antibiotics (9)(10)(11)(12), cationic manganese porphyrins (13,14), chromium (V) complexes (15,16), oxoruthenium complexes (17), UV light (18), and ionizing radiation (19)(20)(21)(22). As shown in Scheme I, 2′ -deoxyribonolactone (dL), an alkaline-labile lesion that is structurally related to an abasic site, is believed to be an intermediate of the C1′ pathway.…”

Section: Introductionmentioning

confidence: 99%

The Release of 5-Methylene-2-Furanone from Irradiated DNA Catalyzed by Cationic Polyamines and Divalent Metal Cations

et al. 2005

View full text Add to dashboard Cite

Release of 5-methylene-2-furanone (5-MF), a characteristic marker of DNA deoxyribose oxidative damage at the C1′ position, was observed in significant quantities from X-irradiated DNA. This observation, which held for DNA irradiated either in aqueous solution or as a film, requires postirradiation treatment at 90° C in the presence of polyamines and divalent metal cations at biological pH. The 5-MF product was quantified by using reverse-phase HPLC. The radiation chemical yield of 5-MF comprised more than 30% of the yield of total unaltered base release. Polylysine, spermine and Be(II) showed the strongest catalytic effect on 5-MF release, while Zn(II), Cu(II), Ni(II), putrescine and Mg(II) were substantially less efficient. We have hypothesized that the 5-MF release from irradiated DNA occurs through catalytic decomposition of the 2′ -deoxyribonolactone (dL) precursor through two consecutive β -and δ -phosphate elimination reactions. A stepwise character of the process was indicated by the S-shaped time course of 5-MF accumulation. If dL proves to be the precursor to 5-MF formation, it would then follow that dL is a very important lesion generated in DNA by ionizing radiation.

show abstract

“…All the products of the scission chemistry are known. They inciude the 3' and 5' phosphomonoester, free bases and 5-methylene furanone (Goyne and Sigman, 1987). These products can be readily accounted for by oxidative attack of a copper-oxo (or copper-bound hydroxyl radical) on the C-1H of the deoxyribose within the minor groove.…”

Section: Op Derivatizatjqqmentioning

confidence: 99%

“…The first step is the identification of a residue in the amino acid sequence which is proximal to the minor groove of DNA but not directiy Involved in high-affinity binding. Accessibility to the minor groove is essential since the C-1H of the deoxyribose, which is the site of oxidative attack by the untargeted 2:1 1,10-phenanthroline-cuprous compiex ((OP)2-Cu*) (Goyne and Sigman, 1987), is the likely target of reaction by the protein-1,10-phenanthroiine chimeras. In the second step, an amino acid residue which satisfies these criteria is then converted into a cysteine using site-directed mutagenesis.…”

Section: Introductionmentioning

confidence: 99%

DNA‐binding proteins as site‐specific nucleases

Pan¹,

Landgraf²,

Sigman³

1994

Molecular Microbiology

Self Cite

View full text Add to dashboard Cite

SummaryDNA-binding proteins can be converted into sitespecific nucleases by linking them to the chemical nuclease 1,10-phenanthroline-copper. This can be readily accomplished by converting a minor grooveproximal amino acid to a cysteine residue using sitedirected mutagenesis and then chemically modifying the sulphydryl group with 5-iodoacetamido-1,10-phenanthroline-copper. These chimeric scission reagents can be used as rare cutters to analyse chromosomai DNA, to test predictions based on high-resoiution nuclear magnetic resonance and X-ray crystal structures, and to locate binding sites of proteins within genomes.

show abstract

Nuclease activity of 1,10-phenanthroline-copper ion. Chemistry of deoxyribose oxidation

Cited by 152 publications

References 1 publication

Structure of the Escherichia coli Fis-DNA complexprobed by protein conjugated with 1,10-phenanthroline copper(I)complex.

Structure of the Escherichia coli Fis-DNA complexprobed by protein conjugated with 1,10-phenanthroline copper(I)complex.

The Release of 5-Methylene-2-Furanone from Irradiated DNA Catalyzed by Cationic Polyamines and Divalent Metal Cations

DNA‐binding proteins as site‐specific nucleases

Contact Info

Product

Resources

About