Stereochemical studies of the .beta.-elimination reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys

Biochemistry ◽  
1991 ◽  
Vol 30 (4) ◽  
pp. 1119-1126 ◽  
Author(s):  
Abhijit Mazumder ◽  
John A. Gerlt ◽  
Michael J. Absalon ◽  
JoAnne Stubbe ◽  
Richard P. Cunningham ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Sodium Hydroxide ◽  
Dna Endonuclease ◽  
Abasic Sites ◽  
Endonuclease Iii ◽  
Beta Elimination ◽  
Elimination Reactions

Oxidative modifications of cellulose in the periodate system – Reduction and beta-elimination reactions

Holzforschung ◽  
2008 ◽  
pp. 090313094857030-- ◽  
Author(s):  
Antje Potthast ◽  
Sonja Schiehser ◽  
Thomas Rosenau ◽  
Mirjana Kostic
Keyword(s):  
System Reduction ◽  
Oxidative Modifications ◽  
Beta Elimination ◽  
Elimination Reactions

scholarly journals Mutational Specificity of the Ferrous Ion in a supF Gene of Endonuclease III/VIII Deficient Escherichia coli.

1997 ◽  
Vol 38 (3) ◽  
pp. 165-171 ◽  
Author(s):  
HIDEO SHIMAMURA ◽  
SUSUMU AKASAKA ◽  
KIHEI KUBO ◽  
YUSUKE SAITO ◽  
SATOSHI NAKAJIMA ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ferrous Ion ◽  
Endonuclease Iii ◽  
Mutational Specificity ◽  
Supf Gene

scholarly journals The Saccharomyces cerevisiae Homologues of Endonuclease III from Escherichia coli, Ntg1 and Ntg2, Are Both Required for Efficient Repair of Spontaneous and Induced Oxidative DNA Damage in Yeast

1999 ◽  
Vol 19 (5) ◽  
pp. 3779-3787 ◽  
Author(s):  
Ingrun Alseth ◽  
Lars Eide ◽  
Manuela Pirovano ◽  
Torbjørn Rognes ◽  
Erling Seeberg ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Dna Damage ◽  
Oxidative Dna Damage ◽  
High Efficiency ◽  
Intracellular Localization ◽  
Genome Project ◽  
Yeast Genome ◽  
Enzyme Analysis ◽  
Endonuclease Iii

ABSTRACT Endonuclease III from Escherichia coli is the prototype of a ubiquitous DNA repair enzyme essential for the removal of oxidized pyrimidine base damage. The yeast genome project has revealed the presence of two genes in Saccharomyces cerevisiae,NTG1 and NTG2, encoding proteins with similarity to endonuclease III. Both contain the highly conserved helix-hairpin-helix motif, whereas only one (Ntg2) harbors the characteristic iron-sulfur cluster of the endonuclease III family. We have characterized these gene functions by mutant and enzyme analysis as well as by gene expression and intracellular localization studies. Targeted gene disruption of NTG1 and NTG2produced mutants with greatly increased spontaneous and hydrogen peroxide-induced mutation frequency relative to the wild type, and the mutation response was further increased in the double mutant. Both enzymes were found to remove thymine glycol and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (faPy) residues from DNA with high efficiency. However, on UV-irradiated DNA, saturating concentrations of Ntg2 removed only half of the cytosine photoproducts released by Ntg1. Conversely, 5-hydroxycytosine was removed efficiently only by Ntg2. The enzymes appear to have different reaction modes, as judged from much higher affinity of Ntg2 for damaged DNA and more efficient borhydride trapping of Ntg1 to abasic sites in DNA despite limited DNA binding. Northern blot and promoter fusion analysis showed that NTG1 is inducible by cell exposure to DNA-damaging agents, whereas NTG2 is constitutively expressed. Ntg2 appears to be a nuclear enzyme, whereas Ntg1 was sorted both to the nucleus and to the mitochondria. We conclude that functions of both NTG1 and NTG2 are important for removal of oxidative DNA damage in yeast.

scholarly journals Multiprobe RNase Protection Assay Analysis of mRNA Levels for the Escherichia coli Oxidative DNA Glycosylase Genes under Conditions of Oxidative Stress

2000 ◽  
Vol 182 (19) ◽  
pp. 5416-5424 ◽  
Author(s):  
Christine M. Gifford ◽  
Jeffrey O. Blaisdell ◽  
Susan S. Wallace
Keyword(s):  
Escherichia Coli ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Mrna Levels ◽  
Aerobic Growth ◽  
Rnase Protection ◽  
Transcript Levels ◽  
Endonuclease Iii ◽  
Base Excision

ABSTRACT Escherichia coli formamidopyrimidine DNA glycosylase (Fpg), MutY DNA glycosylase, endonuclease VIII, and endonuclease III are oxidative base excision repair DNA glycosylases that remove oxidized bases from DNA, or an incorrect base paired with an oxidized base in the case of MutY. Since genes encoding other base excision repair proteins have been shown to be part of adaptive responses inE. coli, we wanted to determine whether the oxidative DNA glycosylase genes are induced in response to conditions that cause the type of damage their encoded proteins remove. The genesfpg, mutY, nei, and nthencode Fpg, MutY, endonuclease VIII, and endonuclease III, respectively. Multiprobe RNase protection assays were used to examine the transcript levels of these genes under conditions that induce the SoxRS, OxyR, and SOS regulons after a shift from anaerobic to aerobic growth and at different stages along the growth curve. Transcript levels for all four genes decreased as cells progressed from log-phase growth to stationary phase and increased after cells were shifted from anaerobic to aerobic growth. None of the genes were induced by hydrogen peroxide, paraquat, X rays, or conditions that induce the SOS response.

scholarly journals A highly conserved endonuclease activity present in Escherichia coli, bovine, and human cells recognizes oxidative DNA damage at sites of pyrimidines.

1987 ◽  
Vol 7 (1) ◽  
pp. 26-32 ◽  
Author(s):  
P W Doetsch ◽  
W D Henner ◽  
R P Cunningham ◽  
J H Toney ◽  
D E Helland
Keyword(s):  
Escherichia Coli ◽  
Dna Damage ◽  
Oxidative Dna Damage ◽  
Uv Light ◽  
Human Fibroblasts ◽  
Human Cells ◽  
Sequence Specificity ◽  
Endonuclease Activity ◽  
E Coli ◽  
Endonuclease Iii

We have compared the sites of nucleotide incision on DNA damaged by oxidizing agents when cleavage is mediated by either Escherichia coli endonuclease III or an endonuclease present in bovine and human cells. E. coli endonuclease III, the bovine endonuclease isolated from calf thymus, and the human endonuclease partially purified from HeLa and CEM-C1 lymphoblastoid cells incised DNA damaged with osmium tetroxide, ionizing radiation, or high doses of UV light at sites of pyrimidines. For each damaging agent studied, regardless of whether the E. coli, bovine, or human endonuclease was used, the same sequence specificity of cleavage was observed. We detected this endonuclease activity in a variety of human fibroblasts derived from normal individuals as well as individuals with the DNA repair deficiency diseases ataxia telangiectasia and xeroderma pigmentosum. The highly conserved nature of such a DNA damage-specific endonuclease suggests that a common pathway exists in bacteria, humans, and other mammals for the reversal of certain types of oxidative DNA damage.

scholarly journals The Repair of DNA Damage Induced in Human Peripheral Lymphocytes with Styrene Oxide

2003 ◽  
Vol 46 (3) ◽  
pp. 95-100 ◽  
Author(s):  
Renata Köhlerová ◽  
Rudolf Štětina
Keyword(s):  
Dna Damage ◽  
Styrene Oxide ◽  
Repair Process ◽  
Dependent Manner ◽  
Peripheral Lymphocytes ◽  
Abasic Sites ◽  
Endonuclease Iii ◽  
Single Strand Breaks ◽  
Human Peripheral Lymphocytes

Isolated human peripheral lymphocytes were treated in vitro with styrene-7, 8–oxide (SO) and the kinetics of the repair of induced DNA damage was assessed by comet assay during further incubation of lymphocytes. Using a modified assay we measured simultaneously the number of single strand breaks in DNA (SSBs) and the sites sensitive to endonuclease III (endo III) that most probably represent abasic sites in DNA molecules. SO induced DNA damage in a dose–dependent manner and both SSBs and endo III sites were removed from the DNA by a repair process with a half time about 2–4 hours. The damage was repaired completely within 12 hours after the treatment.

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