Photoalkylated DNA and ultraviolet-irradiated DNA are incised at cytosines by endonuclease III

Weiss, Randi B.; Duker, Nahum J.

doi:10.1093/nar/14.16.6621

Cited by 44 publications

(34 citation statements)

References 30 publications

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“…Its substrates include a variety of Thy and Cyt residues damaged by ring saturation, fragmentation, or contraction as a result of exposure to ionizing radiation and oxidative agents such as OS04 and permanganate (103)(104)(105)(106) . It has a Krn = 2 X 10-7 M for urea residues in DNA and a kcat = 1 sec-1 for urea and 0.33 sec-1 for thymine glycol (107).…”

Section: Pyrimidine Dimer Dna Gl Ycosylasementioning

confidence: 99%

Dna Repair Enzymes

Sancar

1988

Annu. Rev. Biochem.

811

443

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Section: Pyrimidine Dimer Dna Gl Ycosylasementioning

confidence: 99%

Dna Repair Enzymes

Sancar

1988

Annu. Rev. Biochem.

811

443

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“…Endonuclease III (Endo III) was the first glycosylase discovered to contain this metal cofactor [8]. Endo III removes a wide variety of oxidized pyrimidines from DNA and contains the helixhairpin-helix (HhH) recognition motif [11][12][13][14][15][16][17][18][19]. MutY, structurally similar to Endo III [18][19][20][21], is another BER glycosylase that contains a [4Fe-4S] cluster [20].…”

Section: Introductionmentioning

confidence: 99%

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Boal

Yavin

Barton

2007

Journal of Inorganic Biochemistry

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The [4Fe-4S] cluster is ubiquitous to a class of base excision repair enzymes, in organisms ranging from bacteria to man, and was first considered as a structural element, owing to its redox stability under physiological conditions. When studied bound to DNA, two of these repair proteins (MutY and Endonuclease III from Escherichia coli) display DNA-dependent reversible electron transfer with characteristics typical of high potential iron proteins. These results have inspired a reexamination of the role of the [4Fe-4S] cluster in this class of enzymes. Might the [4Fe-4S] cluster be used as a redox cofactor to search for damaged sites using DNA-mediated charge transport, a process well known to be highly sensitive to lesions and mismatched bases? Described here are experiments demonstrating the utility of DNA-mediated charge transport in characterizing these DNA-binding metalloproteins, as well as efforts to elucidate this new function for DNA as an electronic signaling medium among the proteins.

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“…Endonuclease III (36) is a combined DNA glycosylase (14) and class I AP endonuclease (53) that incises X-irradiated DNA (18,43) and has specificity for thymine glycols, urea residues, and a number of other thymine (6,18,25) and cytosine (16,55) radiolysis products. Exonuclease III (38) is a class II AP endonuclease (8) which accounts for about 90% of the cellular AP activity (57) and, in addition, has associated 3' exonuclease and phosphatase activities (54).…”

mentioning

confidence: 99%

Excision repair of thymine glycols, urea residues, and apurinic sites in Escherichia coli

Laspia

Wallace

1988

J Bacteriol

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The genetic requirements for the excision repair of thymine glycols, urea residues, and apurinic (AP) sites were examined by measuring the survival in Escherichia coli mutants of +X174 replicative form (RF) I transfecting DNA containing selectively introduced lesions. +X RF I DNA containing thymine glycols was inactivated at a greater rate in mutants deficient in endonuclease III (nth) than in wild-type hosts, suggesting that endonuclease Im is involved in the repair of thymine glycols in vivo. +X RF I DNA containing thymine glycols was also inactivated at a greater rate in mutants that were deficient in both exonuclease HI and endonuclease IV (xth nfo) than in wild-type hosts, suggesting that a class II AP endonuclease is required for the in vivo processing of thymine glycols. +X duplex-transfecting DNA containing urea residues or AP sites was inactivated at a greater rate in xth nfo double mutants than in wild-type, but not single-mutant, hosts, suggesting that exonuclease HI or endonuclease IV is required for the repair of these damages and that either activity can substitute for the other. These data are in agreement with the known in vitro substrate specificities of endonuclease III, exonuclease III, and endonuclease IV.Ionizing radiation damages DNA primarily through freeradical reactions which may cause strand breaks, purine or pyrimidine base damages, damage to the deoxyribose moiety, and DNA-DNA or DNA-protein cross-links (23, 52). Since a large variety of DNA damages are produced by ionizing radiation, the determination of the biological consequences of an individual damage that is produced against a background of other damages has been problematic.The use of small, circular, double-stranded DNA bacteriophages, such as 4X174 and PM2, has facilitated the quantitation of X-ray-induced DNA damages and the determination of their biological consequences. Single-strand breaks are produced by X rays in a moderately high yield but appear to be fairly innocuous in repair-proficient hosts (48). Doublestrand breaks are lethal in phages but are produced in low yield (34,48). In bacteriophage PM2 that was X irradiated under oxic conditions, alkali-labile sites were responsible for about 14% of the X-ray-induced lethality, and thymine ring saturation products were responsible for about 5%. Singleand double-strand breaks together account for about 15% of the X-ray-induced lethality (34). This leaves some 66% of the X-ray-induced inactivation caused by unknown alkali-stable base damages. Thymine glycols, urea residues, and apurinic (AP) sites are good models for X-ray-and free radical-induced base and sugar damages (51). Thymine glycols are thymine ring saturation products, and urea residues are fragmentation products of thymine. Both result from the degradation of unstable thymine hydroperoxides which are produced by hydroxyl radical attack on the 5-6 double bond of thymine (47). Thymine glycol is the major stable product produced by the radiolysis of thymine nucleotides (47) and has been found in DNA that was X irra...

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Photoalkylated DNA and ultraviolet-irradiated DNA are incised at cytosines by endonuclease III

Cited by 44 publications

References 30 publications

Dna Repair Enzymes

Dna Repair Enzymes

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Excision repair of thymine glycols, urea residues, and apurinic sites in Escherichia coli

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