1995
DOI: 10.1021/bi00008a018 View full text |Buy / Rent full text
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Abstract: We have measured the fluorescence of the DNA repair enzyme endonuclease III to discover perturbation to its tryptophans by undamaged DNA and AP (apyrimidinic or apurinic) DNA and to estimate binding affinity for intact and AP DNAs. Endonuclease III has two tryptophans, Trp132 in a helix-hairpin-helix region of possible flexibility near the active site for AP lyase activity and Trp178 in the domain containing the iron-sulfur center of endonuclease III; Trp132 is the more solvent-accessible tryptophan [Kuo, C.-F… Show more

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“…If so, the slops of the plots at lower concentrations of copper acetate should be larger than those at higher concentrations of the salt because the fluorophore moieties exposing to the bulk phase are easier to be quenched. A similar observation was frequently found in fluorescence quenching studies of protein conformations [42,43]. Treatment of the quenching data for copper acetate with the modified Stern-Volmer equation [38], a straight line was obtained, which was shown in Fig.…”
Section: Quenching Mechanism Studiessupporting
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rupbmjkragerfmgwileyiopcupepmcmbcthiemesagefrontiersapsiucrarxivemeralduhksmucshluniversity-of-gavle
“…If so, the slops of the plots at lower concentrations of copper acetate should be larger than those at higher concentrations of the salt because the fluorophore moieties exposing to the bulk phase are easier to be quenched. A similar observation was frequently found in fluorescence quenching studies of protein conformations [42,43]. Treatment of the quenching data for copper acetate with the modified Stern-Volmer equation [38], a straight line was obtained, which was shown in Fig.…”
Section: Quenching Mechanism Studiessupporting
“…The retention of specific DNA binding activity by the p26 domain indicates that the structural integrity of the [4Fe-4S] 2ϩ cluster coordinated by four cysteine residues is conserved, thereby providing a surface to interact with DNA, and this region may even serve as a portion of the binding pocket. The above hypothesis is proposed because in endonuclease III, the region containing the [4Fe-4S] 2ϩ cluster has the highest positive electrostatic potential, and this region is implicated in positioning the basic residues for interaction with the phosphate backbone of the DNA substrate (21,23). In addition, based on the location of the iron-sulfur cluster in endonuclease III, models have been built to illustrate its role in DNA binding (24).…”
Section: Discussionmentioning
“…The mutant proteins were expressed in Ecoli UC6444Anth, which carries a deletion of the endonuclease III gene, and purified as described previously (Asahara et al, 1989). The kinetics of the enzymes carrying mutations in the two motifs were determined using an oligonucleotide containing a unique AP site as a substrate (Xing et al, 1995). A duplex l9mer with a 3P label at the 5'-end of the strand containing the AP site was treated with endonuclease III at 37°C in 50 mM HEPES, pH 7.5, 100 mM KCI buffer (O'Handley et al, 1995).…”
Section: Methodsmentioning