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(dA)230*(dT,dU)230
?
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-
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-
?
(pT)7(p(2,3-dihydroxy-5-oxopentyl phosphate))(pT)6
?
-
-
-
-
?
12-mer oligodeoxyribonucleotide containing a 2'-deoxyguanosine at the natural AP site
?
-
-
-
-
?
12-mer oligodeoxyribonucleotide containing a natural AP site
?
-
the minimal kinetic model for the natural AP site incision consists of four stages corresponding to three different transient states of APE1. When the enzyme is complexed with the AP-substrate, the catalytic cycle is completed within 3 s
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?
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site
?
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?
18-mer containing P33-labeled tetrahydrofuran
?
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-
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?
21 bp double-stranded DNA containing an apurinic/apyrimidinic-site analogue
?
-
the affinity of EndoIV for the substrate analogue is very high and its dissociation constant is less than 0.01 microM. A C-terminal DNA-recognition loop at residues 265-269 that is only present in the long type enzymes contributes to its high affinity for apurinic/apyrimidinic sites
-
?
26-bp-oligonucleotide
5'-hexachloro-fluorescein phosphoramidite-labeled 13-mer fragment + ?
oligonucleotide containing a 5'-hexachloro-fluorescein phosphoramidite-labeled tetrahydrofuranyl residue in the middle
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-
?
3'-fluorescein-labeled '-AGTAGACAAG(dU)TACCATGCCTGCACGAAGTT-3'
?
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-
?
3'-fluorescein-labeled 5'-AACTTCGTGCAGGCATGGTAG(dU)TTGTCTACT-3'
?
-
-
-
?
3'-fluorescein-labeled 5'-AGTAGACAAGCTACCATGCCTGCACGAAGTT-3'
?
-
-
-
?
30-mer oligonucleotide duplex DNa containing a tetrahydrofuran analogue
?
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-
-
-
?
31mer oligonucleotide duplex
?
34-mer dsDNA containing an internal tetrahydrofuran
18-mer ds DNA + ?
-
-
-
-
?
34-mer ssDNA containing an internal tetrahydrofuran
18-mer ssDNA + ?
-
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
?
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?
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
?
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?
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
?
-
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
?
-
-
-
-
?
37mer with AP/A
?
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-
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?
37mer with AP/C
?
-
-
-
-
?
37mer with AP/G
?
-
-
-
-
?
37mer with AP/T
?
-
-
-
-
?
37mer with dihydrouridine
?
-
-
-
-
?
43-mer oligonucleotide containing apurinic/apyrimidinic sites
fragments of DNA
-
-
-
?
43-mer oligonucleotide containing the AP-site analog tetrahydrofuran at nt 31
?
-
-
-
-
?
43-mer oligonucleotide containing the AP-site analog THF at nt 31
?
-
-
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?
5'-AACTTCGTGCAGGCATGGG(m6A)TCTTGTCTACT-3'
?
-
-
-
?
5'-AGTAGACAAGATCCCATGCCTGCACGAAGTT-3'
?
-
-
-
?
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
?
-
-
-
?
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
?
-
-
-
?
5'-Cy3-CAAGGTAGTrUATCCTTG-1-Black Hole Quencher1-3'
?
5'-Cy3-CAAGGTAGTTATCCTTG-1-Black Hole Quencher1-3'
?
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
?
-
-
-
?
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
?
-
-
-
?
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
?
alkylated-depurinated DNA
?
-
-
-
-
?
AP DNA
fragments of DNA
-
AP sites
-
-
?
AP-DNA-DNA
?
-
synthetic DNA-DNA hybrid
-
-
?
AP-DNA-RNA
?
-
synthetic DNA-RNA hybrids that simulate a transcription intermediate
-
-
?
c-myc coding region determinant mRNA
?
CAAXACCTTCATCCTTTCC
?
-
X: AP site
-
-
?
CAXAACCTTCATCCTTTCC
?
-
X: AP site
-
-
?
CTAGTCAXCACTGTCTGTGGATAC
?
-
X: AP site
-
-
?
CXAAACCTTCATCCTTTCC
?
-
X: AP site
-
-
?
cytosine-labeled DNA
?
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
?
DNA containing 5,6-dihydrothymidine/A
?
DNA containing 5-hydroxy-2'-deoxyuridine/G
?
DNA containing 5-OH-C/A
?
-
-
-
-
?
DNA containing 5-OH-C/G
?
-
-
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-
?
DNA containing an abasic site
?
-
45-mer oligomer
-
-
?
DNA containing apurinic site
?
DNA containing apurinic sites
?
DNA containing apurinic/apyrimidinic site
?
-
-
-
-
?
DNA containing apurinic/apyrimidinic site
DNA fragments
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-
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-
?
DNA containing apurinic/apyrimidinic sites
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
DNA containing dihydrouracil
?
-
-
-
?
DNA containing dihydrouridine/G
?
-
-
-
-
?
DNA containing O-benzylhydroxylamine
?
-
-
-
-
?
DNA containing O-methylhydroxylamine
?
-
-
-
-
?
DNA containing tamdem dihydrouracil
?
-
the human AP endonuclease APE1 can process the 3' termini generated by human endonuclease III (hNTH) and endonuclease VIII. Both human endonuclease III and endonuclease VIII cannot completely remove both dihydrouracil lesions. With the participation of APE1 and polynucleotide kinase, the 3'-lesions remaining in the products of the reaction with human endonuclease III and endonuclease VIII can efficiently removed. The resulting products can be utilized by repair DNA polymerases as primers for repair synthesis
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?
DNA containing tandem dihydrouracil
?
-
the human AP endonuclease APE1 can process the 3' termini generated by human endonuclease III (hNTH) and endonuclease VIII. Both human endonuclease III and endonuclease VIII cannot completely remove both dihydrouracil lesions. With the participation of APE1 and polynucleotide kinase, the 3'-lesions remaining in the products of the reaction with human endonuclease III and endonuclease VIII can efficiently removed. The resulting products can be utilized by repair DNA polymerases as primers for repair synthesis
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?
DNA containing tetrahydrofuranyl/G
?
DNA containing thymine glycol
?
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?
DNA containing urea
?
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-
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?
DNA with 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
?
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-
?
DNA with 2-deoxyribonolactone
?
-
-
-
-
?
DNA with 5,6-dihydrothymidine/A
?
-
-
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?
DNA with 5,6-dihydrothymine
?
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?
DNA with 5,6-dihydrouracil
?
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-
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?
DNA with 5-hydroxy-2'-deoxyuridine/G
?
-
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?
DNA with 5-hydroxy-5-methylhydantoin
?
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-
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-
?
DNA with 5-hydroxy-6-hydrothymine
?
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?
DNA with 5-hydroxy-6-hydrouracil
?
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-
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?
DNA with alloxan
?
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-
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-
?
DNA with an abasic site
?
DNA with an abasic site
DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde
DNA with dihydrouridine/G
?
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-
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?
DNA with tetrahydrofuranyl/G
?
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?
DNA with thymine glycol
?
-
-
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?
DNA with uracil glycol
?
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-
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?
double-stranded DNA with abasic sites
?
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?
duplex oligonucleotide containing a 5,6-dihydro-2'-deoxyuridine*G pair
?
-
nucleotide incison repair activity
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-
?
duplex oligonucleotide containing a alpha-2'-deoxyadenosine*T pair
?
-
nucleotide incison repair activity
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-
?
duplex oligonucleotide containing a tetrahydrofuran*G pair
?
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nucleotide incison repair activity
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?
GTACGTAXCCACAGACAGTGATGA
?
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X: AP site
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-
?
linear 31-mer duplex oligonucleotide (3'-32P-labeled top strand contains an abasic site at position 17)
3'-32P-labeled 14-mer oligonucleotide
-
cleavage 3' to the apurinic/apyrimidinic site
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-
?
N1 duplex DNA substrate + H2O
?
oligodeoxynucleotide with abasic site 2,3-dihydroxy-5-oxopentyl phosphate
?
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-
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?
oligomer with G/U pair
?
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?
Reactive Blue 2
?
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?
single-stranded DNA with abasic sites
?
-
catalytic efficiency is 20fold less than the activity against double-stranded DNA with abasic sites
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?
THF-containing oligonucleotide
?
thymidine-labeled DNA
?
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-
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?
additional information
?
-
30mer THF-T duplex
?
5'-[32P]labeled 30mer THF-T duplex
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?
30mer THF-T duplex
?
5'-[32P]labeled 30mer THF-T duplex
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-
?
31mer oligonucleotide duplex
?
3'-[alpha-32P]-dAMP-labeled 31mer oligonucleotide duplex
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-
?
31mer oligonucleotide duplex
?
3'-[alpha-32P]-dAMP-labeled 31mer oligonucleotide duplex
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-
?
5'-Cy3-CAAGGTAGTrUATCCTTG-1-Black Hole Quencher1-3'
?
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the fluorogenic substrate OligoI is based on the sequence immediately surrounding the stem V-loop region (OligoI) and incorporating a fluorescent tag, Cy3, at the 5' end and a fluorescence Black Hole Quencher at the 3' end of the oligonucleotide
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?
5'-Cy3-CAAGGTAGTrUATCCTTG-1-Black Hole Quencher1-3'
?
-
the fluorogenic substrate OligoI is based on the sequence immediately surrounding the stem V-loop region (OligoI) and incorporating a fluorescent tag, Cy3, at the 5' end and a fluorescence Black Hole Quencher at the 3' end of the oligonucleotide
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-
?
5'-Cy3-CAAGGTAGTTATCCTTG-1-Black Hole Quencher1-3'
?
-
the fluorogenic substrate DNAOligoI is based on the sequence immediately surrounding the stem Vloop region (OligoI) and incorporating a fluorescent tag, Cy3, at the 5' end and a fluorescence Black Hole Quencher at the 3' end of the oligonucleotide, DNAOligoI has an identical sequence to OligoI except that deoxythymidylate is substituted for 2' hydroxyl uridine
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-
?
5'-Cy3-CAAGGTAGTTATCCTTG-1-Black Hole Quencher1-3'
?
-
the fluorogenic substrate DNAOligoI is based on the sequence immediately surrounding the stem Vloop region (OligoI) and incorporating a fluorescent tag, Cy3, at the 5' end and a fluorescence Black Hole Quencher at the 3' end of the oligonucleotide, DNAOligoI has an identical sequence to OligoI except that deoxythymidylate is substituted for 2' hydroxyl uridine
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-
?
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
?
a synthetic stable AP-site analog where X represents tetrahydrofuran
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?
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
?
a synthetic stable AP-site analog where X represents tetrahydrofuran
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?
AP-DNA
fragments of DNA
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-
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?
AP-DNA
fragments of DNA
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-
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-
?
AP-DNA
fragments of DNA
Base excision repair pathway, enzyme cleaves the 5'-phosphodiester bond, generating 3'-OH and 5'-dRP termini
-
-
?
c-myc coding region determinant mRNA
?
-
APE1 preferentially cleaves in between UA and CA dinucleotides of c-myc coding region determinant RNA
-
-
?
c-myc coding region determinant mRNA
?
-
APE1 preferentially cleaves in between UA and CA dinucleotides of c-myc coding region determinant RNA
-
-
?
c-myc RNA
?
-
APE1 cleaves at the UA, CA, and UG sites of c-myc RNA in vitro
-
-
?
c-myc RNA
?
-
APE1 cleaves at the UA, CA, and UG sites of c-myc RNA in vitro
-
-
?
DNA
fragments of DNA
-
AP endonuclease pE296R has strong preference for mispaired and oxidative base lesions at the 3'-termini of single-strand breaks, the 3'-terminal damaged pyrimidines (uracil, 5,6-dihydrouracil, and 5-hydroxycytosine) are removed with higher efficiency than damaged purines inosine and 7,8-dihydro-8-oxoguanine
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-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
exhibits DNA-glycosylase activity on different types of DNA substrates with pyrimidine damage, being able to release both urea and thymine glycol from double-stranded polydeoxyribonucleotides, also possesses an apurinic/apyrimidinic lyase activity on UV- or gamma-irradiated DNA substrates
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
hydrolyzes phosphodiester bond near heat-induced apruinic sites in double or single strand DNA
-
?
DNA
fragments of DNA
-
hydrolyzes phosphodiester bond near heat-induced apruinic sites in double or single strand DNA
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?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
breaks strand on the 3'-side of apurinic sugar residues giving a 3'-OH and a 5'-phosphate
-
?
DNA
fragments of DNA
-
The latter lesions are processed by AP endonucleases, which are important components of the base excision repair pathway
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-
?
DNA
fragments of DNA
-
-
-
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?
DNA
fragments of DNA
-
-
-
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?
DNA
fragments of DNA
-
removes UV light and osmium tetroxide damaged bases via an N-glycosylase activity followed by a 3'-purinic/apyrimidinic endonuclease activity, product is a nucleoside-free site flanked by 3'- and 5'-terminal phosphate groups
-
?
DNA
fragments of DNA
-
incises DNA damaged with UV light, ionizing radiation, OsO4, KMnO4 and H2O2 at cytosine and thymine sites
-
?
DNA
fragments of DNA
-
specific for DNA containing either apurinic or apyrimidinic sites
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
specific for DNA containing either apurinic or apyrimidinic sites
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
dU)230 (ratio dT:dU is 15) partially depyrimidinated by uracil-DNA glycosylase
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?
DNA
fragments of DNA
-
alkylated-depurinated DNA
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
AP endonuclease I forms deoxyribose 3'-phosphate and 5'-OH termini upon cleaving depurinated DNA
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
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?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
cleavage at abasic sites in duplexes with paired lesions is slower than in duplexes with single lesions. Double strand breaks are readily generated in duplexes with abasic sites positioned 3' to each other. In duplexes containing abasic sites set 1 base pair apart, 5' to each other, both enzymes slowly cleave the abasic site on one strand only and are unable to incise the other stand
-
?
DNA
fragments of DNA
-
removes 5-hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine via a N-glycosylase/beta-elimination reaction
-
?
DNA
fragments of DNA
-
cuts the DNA strands on the 5' side of the apurinic sites giving a 3'-OH and a 5'-phosphate
-
?
DNA
fragments of DNA
-
endonucleolytic cleavage near apurinic or apyrimidinic sites to products with 5'-phosphates, e.g. UV-irradiated poly(dA)*poly(dT)
-
?
DNA
fragments of DNA
-
catalyzes phosphodiester bond cleavage via a lyase- rather than a hydrolase mechanism
-
?
DNA
fragments of DNA
-
synthetic oligodeoxynucleotides containing abasic sites
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
endonuclease III: excision of a number of thymine- and cytosine-derived lesions from DNA, no purine-derived lesions excised by endonuclease III
-
?
DNA
fragments of DNA
-
endonucleolytic activity against apurinic and apyrimidinic sites and a dose-dependent response to DNA that has been X-irradiated, UV-irradiated or treated with OsO4
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
duplex oligonucleotides containing the base lesion analogs O-methylhydoxylamine or O-benzylhydroxylamine, N-glycosylase activity generates intermediary AP site which is subsequently cleaved by the enzyme -associated AP lyase activity, O-alkoxyamine-modified AP sites are poorer substrates than the presumed physiological substrates
-
?
DNA
fragments of DNA
-
enzyme generates only single-strand breaks when the base damage is set one and three base-pairs apart, and only slowly introduces double-strand breaks in substrates where base damage is set five or seven base-pairs apart. Treatment of an abasic site-containing DNA readily yields double-strand breaks.
-
?
DNA
fragments of DNA
-
DNA containing dihydrouridine, 5,3-dihydrothymidine, 5-hydroxy-2'-deoxyuridine, 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine or tetrahydrofuranyl
-
?
DNA
fragments of DNA
-
the beta-elimination reaction breaking the C3'-O-P bond 3' to an AP site can be followed by a delta-elimination reaction breaking the C5'-O-P bond 5' to the AP site, with the release of an unsaturated derivative of the base-free sugar and the generation of a gap flanked by 3'-phosphate and 5'-phosphate ends
-
?
DNA
fragments of DNA
-
recognizes urea, an oxidative ring fragmentation product of thymine
-
?
DNA
fragments of DNA
-
when DNA containing thymine glycol is used as substrate the combined N-glycosylase/AP endonuclease activity is about 2fold higher than the AP endonuclease activity
-
?
DNA
fragments of DNA
-
KsgA has al DNA glycosylase/AP lyase activity for C mispaired with oxidized T
-
-
?
DNA
fragments of DNA
-
KsgA has al DNA glycosylase/AP lyase activity for C mispaired with oxidized T
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
648685, 648686, 648687, 694298, 701749, 702317, 702939, 703032, 703960, 704663, 704731, 704948, 705736, 706019, 706429 -
-
?
DNA
fragments of DNA
-
-
?
DNA
fragments of DNA
-
-
?
DNA
fragments of DNA
-
-
?
DNA
fragments of DNA
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
cleavage of apyrimidinic DNA both 5' and 3' to the site of damage in a ratio of 60:40, respectively, even though it can cleave on both sides of an internal apyrimidinic site, it does not release deoxyribose 5-phosphate from terminal apyrimidinic sites
-
?
DNA
fragments of DNA
-
acts on specific adenines in single-stranded DNA
-
?
DNA
fragments of DNA
-
cleaves single- and double-stranded oligonucleotides lacking one or two bases
-
?
DNA
fragments of DNA
enzyme reveals glycosylase activity and apurinic/apyrimidinic lyase activity on duplex DNA containing 8-OH-G, DNA containing 8-OH-G/A is not cleaved, DNA containing 8-OH-G/T and 8-OH-G/G is slightly cleaved
-
?
DNA
fragments of DNA
-
cleavage at abasic sites in duplexes with paired lesions is slower than in duplexes with single lesions. Double strand breaks are readily generated in duplexes with abasic sites positioned 3' to each other. In duplexes containing abasic sites set 1 base pair apart, 5' to each other, both enzymes slowly cleave the abasic site on one strand only and are unable to incise the other stand
-
?
DNA
fragments of DNA
-
acts on both 5-hydroxycytosine and abasic sites, preferentially when these are situated opposite guanines
-
?
DNA
fragments of DNA
-
catalyzes incision at the C4-keto-C-1-aldehyde site, hydrolyzes 3'-phosphoglycolates 25fold more slowly than C-4-keto-C-1-aldehydes
-
?
DNA
fragments of DNA
-
cleaves the DNA phosphodiester backbone immediately 5' to an AP site, also shows 3'-phosphodiesterase activity, 3'-phosphatase activity, RNaseH and significant 3'-5'-exonuclease activity
-
?
DNA
fragments of DNA
-
catalyzes 5'-incision of 2-deoxyribonolactone, but acts at least 10fold less effectively to remove the 3'-phosphates at direct strand breaks
-
?
DNA
fragments of DNA
cleaves thymine glycol-containing form I plasmid DNA and a dihydrouracil-containing oligonucleotide duplex
-
?
DNA
fragments of DNA
-
rate of AP lyase-mediated strand cleavage is much slower than the rate of DNA N-glycoxsylase-mediated base release
-
?
DNA
fragments of DNA
-
specific for DNA containing either apurinic or apyrimidinic sites
-
?
DNA
fragments of DNA
-
endonuclease A: activity for UV-irradiated DNA, gamma-irradiated DNA and OsO4-treated DNA
-
?
DNA
fragments of DNA
base excision repair (BERa) pathway is initiated by lesion-specific glycosylases that excise the damaged base from the sugar-phosphate backbone, resulting in a potentially cytotoxic apurinic/apyrimidinic (AP) site intermediate that becomes the substrate for the major human AP endonuclease
-
-
?
DNA
fragments of DNA
-
bifunctional enzyme is involved in base excision repair, it is a bifunctional DNA glycosylase/apurinic/apyrimidinic lyase which removes hydrated, reduced, or oxidized bases from the DNA backbone as the initial step of base excision repair
-
-
?
DNA
fragments of DNA
-
DNA single-strand breaks containing 3'-blocking groups are generated from attack of the sugar backbone by reactive oxygen species or after base excision by DNA glycosylase/apurinic/apyrimidinic (AP) lyases
-
-
?
DNA
fragments of DNA
-
5'-deoxyribose-5-phosphate and apurinic/apyrimidinic sites are excised with half-lives of 2.7 and 7.0 min, respectively
-
-
?
DNA
fragments of DNA
-
Ape1 cleaves the phosphodiester backbone 5' to the AP site generating 3'-hydroxyl and 5'-deoxyribosephosphate termini, Ape1 exhibits a prominent 5' hydrolytic AP endonuclease, a weak 3'-diesterase and a 3'-5'-exonuclease activity
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
at low concentrations the enzyme is specific for depurinated native DNA, at higher concentrations it degrades DNA in a non-specific manner
-
?
DNA
fragments of DNA
-
DNA single-strand breaks containing 3'-blocking groups are generated from attack of the sugar backbone by reactive oxygen species or after base excision by DNA glycosylase, apurinic, apyrimidinic (AP) lyases
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
acts specifically on pyrimidine dimers, preferring those in double-stranded DNA to those in singes-stranded DNA, enzyme has glycosylase and apyrimidinic/apurinic endonuclease activity, cleaves 3' to the AP site generating a 3'-deoxyribose moiety and a 5'-phosphate
-
?
DNA
fragments of DNA
-
phage-T4 and Micrococcus luteus enzyme nick the C(3')-O-P-bond 3' to the apurinic/apyrimidinic sites in DNA, the phage enzyme can also subsequently nick the C(5')-O-P bond 5' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
supercoiled DNA
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
enzyme recognizes apurinic and apyrimidinic sites induced by acid and gamma-rays, as well as lesions which are introduced into DNA by UV irradiation and OsO4
-
?
DNA
fragments of DNA
thymine glycol DNA glycosylase, urea DNA glycosylase and AP lyase activity
-
?
DNA
fragments of DNA
-
no activity with methylated or OsO4-treated DNA
-
?
DNA
fragments of DNA
-
enzyme plays an important role in oxidative signalling, transcription factor regulation, and cell cycle control
-
-
ir
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
cleaves phosphodiester bridge wihich is the immediate neighbor of the AP site on its 5' side leaving 3'-OH and 5'-phosphate ends
-
?
DNA
fragments of DNA
-
PM2 phage DNA
-
?
DNA
fragments of DNA
-
DNA repair enzyme is involved in base excision repair of apurinic/apyrimidinic sites after oxidative DNA damage
-
-
?
DNA
fragments of DNA
-
multifunctional enzyme involved in DNA base excision repair of oxidative DNA damage and in redox regulation of a number of transcription factors
-
-
?
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
cleaves all four types of abasic site-containing substrates: AP/G, AP/A, AP/C, AP/T, with a moderate preference for AP/T sites
-
?
DNA
fragments of DNA
-
cuts the DNA strands on the 5' side of the apurinic sites giving a 3'-OH and a 5'-phosphate
-
?
DNA
fragments of DNA
-
catalyzes the hydrolysis of the 5'-phosphodiester bond at the abasic site
-
?
DNA
fragments of DNA
-
recognizes and cleaves DNA substrates containing dihydrouracil, 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine and abasic sites, but not DNA substrates containing uracil or 8-oxoguanine
-
?
DNA
fragments of DNA
-
DNA containing dihydrouridine, 5,3-dihydrothymidine, 5-hydroxy-2'-deoxyuridine, 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine or tetrahydrofuranyl
-
?
DNA
fragments of DNA
-
oxidative DNA damage is primarily reversed by the base excision repair pathway, initiated by N-glycosylase apurinic/apyrimidinic lyase proteins
-
-
ir
DNA
fragments of DNA
-
-
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
enzyme has a 3' to 5' exonuclease activity and shows additional functional similarities to DNA repair enzymes
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
-
-
-
-
?
DNA
fragments of DNA
-
enzyme has a 3' to 5' exonuclease activity and shows additional functional similarities to DNA repair enzymes
-
?
DNA
fragments of DNA
-
specific for apurinic sites
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
-
-
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
-
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
-
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
-
-
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
endonucleolytic cleavage near apurinic or apyrimidinic sites to products with 5'-phosphates, e.g. UV-irradiated poly(dA)*poly(dT)
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
catalyzes phosphodiester bond cleavage via a lyase- rather than a hydrolase mechanism
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
duplex oligonucleotides containing the base lesion analogs O-methylhydoxylamine or O-benzylhydroxylamine, N-glycosylase activity generates intermediary AP site which is subsequently cleaved by the enzyme -associated AP lyase activity, O-alkoxyamine-modified AP sites are poorer substrates than the presumed physiological substrates
-
?
DNA
fragments of DNA
Tequatrovirus T4
-
phage-T4 and Micrococcus luteus enzyme nick the C(3')-O-P-bond 3' to the apurinic/apyrimidinic sites in DNA, the phage enzyme can also subsequently nick the C(5')-O-P bond 5' to the apurinic/apyrimidinic site
-
?
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
?
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
?
-
-
-
-
?
DNA containing 5,6-dihydrothymidine/A
?
-
-
-
-
?
DNA containing 5,6-dihydrothymidine/A
?
-
-
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine/G
?
-
-
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine/G
?
-
-
-
-
?
DNA containing apurinic site
?
-
-
-
-
?
DNA containing apurinic site
?
-
-
-
-
?
DNA containing apurinic sites
?
-
-
-
-
?
DNA containing apurinic sites
?
-
-
-
-
?
DNA containing apurinic/apyrimidinic sites
?
-
-
-
?
DNA containing apurinic/apyrimidinic sites
?
-
-
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
apurinic/apyrimidinic endonuclease Nfo protects Bacillus subtilis spores from DNA damage accumulated during spore dormancy
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
specificity
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
C4'-oxidized abasic sites are efficiently excised via intermediate Schiff-base formation. Activity is 100fold less efficient than repair by exonuclease III
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
endonuclease III plays an important cellular role by removing premutagenic pyrimidine damages produced by reactive oxygen species. EcoNth is a bifunctional enzyme that has DNA glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
the enzyme forms a Schiff base-type intermediate with the substrate after the damaged base is removed
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
hydrogen bonds to phosphate groups 3' to the cleavage site is essential for the binding of the enzyme to the product DNA, which may be necessary for efficient functioning of the base excision rapair pathway
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
inducible enzyme, the enzyme exhibits endonucleolytic activity and is regulated as part of the acid-adaptive response of the organism. Smx is likely the primary, if not the sole, AP endonuclease induced during growth at low pH values, loss of Smx activity renders the mutant strain sensitive to hydrogen peroxide treatment but relatively unaffected by acid-mediated damage or near-UV irradiation
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
inducible enzyme, the enzyme exhibits endonucleolytic activity and is regulated as part of the acid-adaptive response of the organism. Smx is likely the primary, if not the sole, AP endonuclease induced during growth at low pH values, loss of Smx activity renders the mutant strain sensitive to hydrogen peroxide treatment but relatively unaffected by acid-mediated damage or near-UV irradiation
-
-
?
DNA containing tetrahydrofuranyl/G
?
-
-
-
-
?
DNA containing tetrahydrofuranyl/G
?
-
-
-
-
?
DNA with an abasic site
?
the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone
-
-
?
DNA with an abasic site
?
the enzyme has little specificity for the base opposite 8-oxoguanine. The enzyme has both DNA glycosylase and DNA lyase (beta-elimination) activity, and the combined glycosylase/lyase activity occurs at a rate comparable with the glycosylase activity alone
-
-
?
DNA with an abasic site
?
-
-
-
?
DNA with an abasic site
?
the enzyme is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA with an abasic site
?
the substrate specificity for 8-oxoguanine/guanine sites is higher than that for 8-oxoguanine/cytosine sites. apurinic-lyase activity of this enzyme cleaved only 20% of these apurinic-sites at the same time point
-
-
?
DNA with an abasic site
?
-
-
-
?
DNA with an abasic site
?
the enzyme is part of the base excision repair (BER) pathway. It protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine, from single- and double-stranded DNA substrates
-
-
?
DNA with an abasic site
?
the substrate specificity for 8-oxoguanine/guanine sites is higher than that for 8-oxoguanine/cytosine sites. apurinic-lyase activity of this enzyme cleaved only 20% of these apurinic-sites at the same time point
-
-
?
DNA with an abasic site
DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde
the enzyme excises an oxidatively-damaged form of guanine. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities
-
-
?
DNA with an abasic site
DNA with 5'-phosphate terminus + DNA with 3'-alpha,beta-unsaturated aldehyde
bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities. The specificity of DNA glycosylase activity of is compared using 39-mer DNA duplexes containing an 8-oxoG residue opposite each of the four natural DNA bases (A, T, G and C). The enzyme efficiently cleaves oligomers containing 8-oxoG:C and 8-oxoG:G base pairs, less effective on oligomers containing 8-oxoG:T and 8-oxoG:A mispairs. The enzyme catalyzes a beta-elimination reaction at the apurinic site produced by excision of the 8-oxoguanine and thus generates a 5'-phosphate terminus and a 3'-alpha,beta-unsaturated aldehyde sugar terminus at the incision site. Bifunctional enzyme with both DNA glycosylase and apurinic/apyrimidinic lyase activities
-
-
?
N1 duplex DNA substrate + H2O
?
5'-FAM peptide-labelled AP DNA duplex substrate
-
-
?
N1 duplex DNA substrate + H2O
?
5'-FAM peptide-labelled AP DNA duplex substrate
-
-
?
N1 duplex DNA substrate + H2O
?
5'-FAM peptide-labelled AP DNA duplex substrate
-
-
?
THF-containing oligonucleotide
?
-
AP endonuclease activity
-
-
?
THF-containing oligonucleotide
?
-
AP endonuclease activity
-
-
?
additional information
?
-
major role in plant defence against oxidative DNA damage
-
-
?
additional information
?
-
-
major role in plant defence against oxidative DNA damage
-
-
?
additional information
?
-
-
no substrate: alkylated sites
-
-
?
additional information
?
-
-
no substrate: alkylated sites
-
-
?
additional information
?
-
-
no substrate: native DNA
-
-
?
additional information
?
-
-
no substrate: native DNA
-
-
?
additional information
?
-
-
DNA polymerase X, along with polymerization and 3'-5'-exonuclease activities, possesses an intrinsic abasic endonuclease activity. Both, abasic endonuclease and 3'-5'-exonuclease activities are genetically linked and governed by the same metal ligands located at the C-terminal polymerase and histidinol phosphatase domain of the polymerase
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
important role in repair of oxidative DNA damage
-
-
?
additional information
?
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
no activity with DNA that has been damaged by UV light, methyl methanesulfonate, osmium teroxide or sodium bisulfite
-
-
?
additional information
?
-
-
enzyme has an essential base excision repair (BER) activity and a redox activity that regulates expression of a number of genes through reduction of their transcription factors, AP-1, NFkappaB, HIF-1alpha, CREB, p53 and others
-
-
?
additional information
?
-
-
no substrate: alkylated sites
-
-
?
additional information
?
-
-
no substrate: native DNA
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
all known bacterial AP lyases and some at least of the mammalian ones, also acts as DNA glycosylases
-
-
?
additional information
?
-
-
bacteriophage T4 endonuclease V and Escherichia coli endonuclease II catalyze N-glycosylase and 3'-abasic endonuclease reaction, beta-elimination reaction
-
-
?
additional information
?
-
-
no substrate: alkylated sites
-
-
?
additional information
?
-
-
no substrate: native DNA
-
-
?
additional information
?
-
-
pdT8d(-)dTn is cleaved by endonuclease III yielding two products which have the same electrophoretic behaviour as the doublet obtained by alkaline beta-elimination, thus the enzyme is a beta-elimination catalyst
-
-
?
additional information
?
-
-
KsgA does not remove C opposite normal bases, 7,8-dihydro-8-oxoguanine and 2-hydroxyadenine, KsgA does not excise thymine glycol, 5-formyluracil, and 5-hydroxymethyluracil opposite cytosine from double-stranded oligonucleotides
-
-
?
additional information
?
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
additional information
?
-
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
additional information
?
-
analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III using oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analogue, and undamaged duplexes carried fluorescent DNA base analogues 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups, pre-steady-state kinetic analysis, overview. Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. The glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as DNA lesion sensors
-
-
?
additional information
?
-
-
analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III using oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analogue, and undamaged duplexes carried fluorescent DNA base analogues 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups, pre-steady-state kinetic analysis, overview. Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. The glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as DNA lesion sensors
-
-
?
additional information
?
-
-
enzymatic repair of abasic sites, key intermediate step in base excision repair pathway
-
-
?
additional information
?
-
-
KsgA does not remove C opposite normal bases, 7,8-dihydro-8-oxoguanine and 2-hydroxyadenine, KsgA does not excise thymine glycol, 5-formyluracil, and 5-hydroxymethyluracil opposite cytosine from double-stranded oligonucleotides
-
-
?
additional information
?
-
-
no substrate: alkylated sites
-
-
?
additional information
?
-
-
no substrate: native DNA
-
-
?
additional information
?
-
enzyme HpXth removes the AP site, 3'-blocking sugar-phosphate, and 3'-terminal phosphate in DNA strand breaks with good efficiency (kcat/KM = 1.240, 0.044, and 0.0054 mM/min, respectively). In the presence of 1 or 5 mM Mg2+ or Mn2+, the purified recombinant His-tagged HpXth protein exerts an efficient AP site cleavage activity by generating fast-migrating 10mer cleavage fragments. 3'-Repair phosphodiesterase, 3'-phosphatase, and nucleotide incision activities of the HpXth protein, overview
-
-
?
additional information
?
-
-
enzyme HpXth removes the AP site, 3'-blocking sugar-phosphate, and 3'-terminal phosphate in DNA strand breaks with good efficiency (kcat/KM = 1.240, 0.044, and 0.0054 mM/min, respectively). In the presence of 1 or 5 mM Mg2+ or Mn2+, the purified recombinant His-tagged HpXth protein exerts an efficient AP site cleavage activity by generating fast-migrating 10mer cleavage fragments. 3'-Repair phosphodiesterase, 3'-phosphatase, and nucleotide incision activities of the HpXth protein, overview
-
-
?
additional information
?
-
enzyme HpXth removes the AP site, 3'-blocking sugar-phosphate, and 3'-terminal phosphate in DNA strand breaks with good efficiency (kcat/KM = 1.240, 0.044, and 0.0054 mM/min, respectively). In the presence of 1 or 5 mM Mg2+ or Mn2+, the purified recombinant His-tagged HpXth protein exerts an efficient AP site cleavage activity by generating fast-migrating 10mer cleavage fragments. 3'-Repair phosphodiesterase, 3'-phosphatase, and nucleotide incision activities of the HpXth protein, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
gelonin, pokeweed antiviral protein and ricin belong to the family of ribosome-inactivating proteins with DNA-glycosylase/AP-lyase activities
-
-
?
additional information
?
-
-
unlike other endonucleases endonuclease IV or Exo III, Ape1 does not enhance the rate of product release with a G/A substrate
-
-
?
additional information
?
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme has no biologically significant 3'-5'-exonuclease activity, the activity only manifests at enzyme concentrations elevated by 6-7 orders magnitude, activity does not show a preference to mismatched compared to matched DNA structures as well as to nicked or gapped DNA substrates
-
-
?
additional information
?
-
enzyme lacks 3'-endonuclease activity against undamaged DNA
-
-
?
additional information
?
-
-
enzyme lacks 3'-endonuclease activity against undamaged DNA
-
-
?
additional information
?
-
-
enzyme stimulates polymerase beta activity on the 5'-terminal oxidized abasic residue
-
-
?
additional information
?
-
-
corrects apurinic/apyrimidinic sites in the genome
-
-
?
additional information
?
-
-
multifunctional enzyme involved in DNA repair and redox regulation of transcription factors
-
-
?
additional information
?
-
-
key enzyme in repair of oxidatively damaged DNA
-
-
?
additional information
?
-
catalyses the initial step in apruinic/apyrimidinic site repair
-
-
?
additional information
?
-
-
catalyses the initial step in apruinic/apyrimidinic site repair
-
-
?
additional information
?
-
-
enzyme stimulates long patch base excision repair by cleaving the DNA and then facilitating the sequential binding and catalysis by DNA polymerase beta, DNA polymerase delta, FEN1 and DNA ligase I
-
-
?
additional information
?
-
-
AP endonuclease Ape1 is involved in the nucleotide incision repair pathway
-
-
?
additional information
?
-
-
APE1 exonuclease function appears to be modulated by the other BER proteins DNA polymerase beta and poly(ADP-ribose) polymerase 1. Excess APE1 over DNA polymerase beta may allow APE1 to perform both exonuclease function and stimulation of strand-displacement DNA synthesis by DNA polymerase beta
-
-
?
additional information
?
-
-
the enzyme enhances methylpurine-DNA glycosylase-catalyzed excision, complex formation of methylpurine-DNA glycosylase eith proliferating cell nuclear antigen can accomodate binding of APE1
-
-
?
additional information
?
-
-
the function of APE is considered as the rate-limiting step in DNA base excision repair. AP endonuclease suppresses DNA mismatch repair activity leading to microsatellite instability
-
-
?
additional information
?
-
hOgg1 protein catalyzes the excision of 8-oxo-7,8-dihydroguanine and the incision of apurinic and apyrimidinic sites in DNA
-
-
?
additional information
?
-
-
hOgg1 protein catalyzes the excision of 8-oxo-7,8-dihydroguanine and the incision of apurinic and apyrimidinic sites in DNA
-
-
?
additional information
?
-
-
the enzyme remains bound to its incision product when the 5'-incision us in double-stranded DNA. The enzyme dissociates from its single-stranded 5'-incised product
-
-
?
additional information
?
-
-
a DNA base excision repair enzyme with a wide variety of functions, including AP endonuclease (cleaving an AP site 5' to a deoxyribose phosphate moiety), 3' exonuclease, 3' phosphodiesterase, 3' phosphatase, RNaseH, and 5' endonuclease activities
-
-
?
additional information
?
-
-
AP endo acts by a one-step associative phosphoryl transfer mechanism on a THF-containing substrate
-
-
?
additional information
?
-
-
AP endo acts on many types of DNA substrate molecules but demonstrates the most robust activity when acting as a class II AP endonuclease
-
-
?
additional information
?
-
-
APE/Ref-1 is a critical component of the hypoxia-inducible transcriptional complex that interacts with hypoxia-inducible factor-1 and p300
-
-
?
additional information
?
-
-
APE/Ref-1 is a key regulator, it markedly induces and efficiently protects melanocytes from oxidative damage by inducing the antiapoptotic machinery and stimulating cell survival
-
-
?
additional information
?
-
APE1 appears to have endonucleolytic activity as a repair enzyme within the nucleotide incision repair pathway
-
-
?
additional information
?
-
-
APE1 appears to have endonucleolytic activity as a repair enzyme within the nucleotide incision repair pathway
-
-
?
additional information
?
-
-
APE1 can incise DNA at the 5'-position of oxidized pyrimidine bases such as 5,6-dihydro-thymine or 5,6-dihydro-2'-deoxyuracil (DHU), thus initiating a repair process known as nucleotide incision repair (NIR)
-
-
?
additional information
?
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APE1 has been identified as a protein capable of nuclear redox activity, inducing the DNA binding activity of several transcription factors, such as activator protein-1, nuclear factor-kappaB, Myb, polyoma virus enhancer-binding protein-2, HLF, nuclear factor-Y, early growth response protein-1, hypoxia inducible factor-1alpha, ATF/CREB family, p53, and Pax proteins. In each case, this effect is accomplished by maintaining the cysteine residues of the transcription factors in the reduced state.
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APE1 has DNA 3'-phosphatase activity in vitro and 3' to 5' exonuclease activity, which could be physiologically relevant in the removal of mismatched or damaged nucleotides incorporated during the synthesis step of BER
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Ape1 has the ability to incise at AP sites in DNA conformations formed during DNA replication, transcription, and class switch recombination, and that Ape1 can endonucleolytically destroy damaged RNA
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APE1 hydrolytically cleaves the phosphodiester backbone 5' to the AP site, leaving a 3'-hydroxyl and a 5'-abasic deoxyribose phosphate to be processed by the subsequent cascade of BER enzymes
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APE1 hydrolytically cleaves the phosphodiester backbone 5' to the AP site, leaving a 3'-hydroxyl and a 5'-abasic deoxyribose phosphate to be processed by the subsequent cascade of BER enzymes
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APE1 is a fundamental protein in this essential repair pathway and is thought to be responsible for more than 95% of total AP endonuclease activity in human cell culture extracts
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APE1 is a fundamental protein in this essential repair pathway and is thought to be responsible for more than 95% of total AP endonuclease activity in human cell culture extracts
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Ape1 is a multifunctional enzyme of 318 amino acids with redox-dependent regulation of transcription factors, 3' to 5' exonuclease, 3' phosphodiesterase, RNaseH and class II type AP endonuclease activities
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APE1 is also named as redox effector factor-1 because of its redox abilities on different redox-regulated transcription factors
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APE1 is directly responsible for the control of the intracellular ROS levels through its inhibitory effect on Rac1, the regulatory subunit of a membrane nonphagocytic NADPH oxidase system.
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APE1 recognizes AP sites in DNA that arise either spontaneously or as enzymatic products of DNA repair glycosylases that excise substrate base lesions as part of the base excision repair (BER) response. Subsequent to damage recognition, the chemistry central to the function of APE1 is wateractivated by a Mg2+ ion followed by hydrolytic cleavage of the phosphodiester bond immediately 5' to the abasic site
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APE1 utilizes a site located in its N-terminus for redox regulation of important transcription factors such as NF-kappaB, p53, c-Fos, and c-Jun
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APE1 utilizes a site located in its N-terminus for redox regulation of important transcription factors such as NF-kappaB, p53, c-Fos, and c-Jun
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APE1/Ref-1 also has a complex relationship to high-mobility group box 1, a protein secreted by immune cells in response to inflammatory stimuli. APE1/Ref-1 can both promote and suppress inflammatory signaling induced by high-mobility group box 1
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APE1/Ref-1 plays a complex role in the activation of nuclear factor kappa B, a key transcription factor involved in inflammatory and immune signaling
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APE1/Ref-1 plays a role in cardiovascular physiology and pathophysiology. APE1/Ref-1 suppresses myocardial ischemia-reperfusion injury and vascular inflammation, and promotes endothelium-dependent vascular relaxation
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APE1/Ref-1 promotes the effect of angiotensin II on Ca2+-activated K+-channel in human endothelial cells via suppression of NADPH oxidase
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APE1/Ref-1 reduces oxidative stress by regulating the level of reactive oxygen species in the cytoplasm
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APEs have 2 intrinsic activities in DNA repair. They act as an endonuclease in cleaving AP sites to generate 3' OH and 5' phosphodeoxyribose termini. They also act as a 3' phosphodiesterase/exonuclease to remove 3' blocking phosphodeoxyribose or its fragments generated during strand breaks, and by reactive oxygen species or DNA glycosylases that excise oxidized bases in the first step of base excision repair
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enzyme cleaves the AP sites in DNA and allows them to be repaired by other enzymes involved in base excision repair
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enzyme has an essential base excision repair (BER) activity and a redox activity that regulates expression of a number of genes through reduction of their transcription factors, AP-1, NFkappaB, HIF-1alpha, CREB, p53 and others
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enzyme has the ability to reductively activate redoxsensitive transcription factors and negative gene regulation by extracellular calcium
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enzyme stimulates the DNA binding activity of the AP-1 family of transcription factors via a redox-dependent mechanism
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forced cytoplasmic overexpression of APE1 profoundly attenuates the upregulation of high-mobility group box 1-mediated reactive oxygen species generation, cytokine secretion, and cyclooxygenase-2 expression by primary monocytes and macrophage-like THP-1 cell lines
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high-mobility group box 1-induced activation of p38 and c-Jun N-terminal kinase is strongly abrogated by the overexpression of APE1
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hNTH1 and Y-box-binding protein-1 may be part of the same DNA repair pathway in response to cisplatin and UV treatments
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hNTH1 binds directly to Y-box-binding protein-1 in the absence of nucleic acids, it binds to the auto-inhibitory n-terminal tail of NTH1
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human Ape1 is a multifunctional protein with a major role in initiating repair of apurinic/apyrimidinic (AP) sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage
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human apurinic/apyrimidinic endonuclease 1 is a major constituent of the base excision repair (BER) pathway of AP sites of DNA lesions. APE1 specifically binds to abasic sites and cuts the 5'-phosphodiester bond with its endonuclease activity to produce a DNA primer with 3'-hydroxyl end, which is a required step in the BER repair pathway
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human endonuclease III is a relevant target to potentiate cisplatin cytotoxicity in Y-box-binding protein-1 overexpressing tumor cells
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In addition to its primary AP site incision function, APE1 exhibits 3'-5' exonuclease, 3'-phosphodiesterase and RNase H catalysis, and a 3'-phosphatase activity
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In addition to its primary AP site incision function, APE1 exhibits 3'-5' exonuclease, 3'-phosphodiesterase and RNase H catalysis, and a 3'-phosphatase activity
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In addition to the exonuclease function, human APE1 is endowed with another enzymatic activity potentially relevant for the protection against oxidative damage
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In human cells, APE1 excises sugar fragments that block the 3'-ends thus facilitating DNA repair synthesis
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major factor in the maintenance of the integrity of the human genome
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multifunctional protein involved in base excision DNA repair and in transcriptional regulation of gene expression, importance to genomic stability and cell survival
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multifunctional protein involved in reduction-oxidation regulation. It functions as a redox factor that maintains transcription factors in an active reduced state
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multifunctional protein possessing both DNA repair and transcriptional regulatory activities, has a pleiotropic role in controlling cellular response to oxidative stress. APE1 is the main apurinic/apyrimidinic endonuclease in eukaryotic cells, playing a central role in the DNA base excision repair pathway of all DNA lesions (uracil, alkylated and oxidized, and abasic sites), including single-strand breaks, and has also co-transcriptional activity by modulating genes expression directly regulated by either ubiquitous and tissue specific transcription factors. It controls the intracellular redox state by inhibiting the reactive oxygen species production
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overexpression of APE1/Ref-1 suppressed angiotensin II induced production of superoxide and hydrogen peroxide
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small interfering RNA knockdown of endogenous APE1 impairs high-mobility group box 1-mediated cytokine expression and MAPK activation in THP-1 cells. High-mobility group box 1-stimulation induces the translocation of APE1 to the nucleus of the cell
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The BK-Ca current in APE1/Ref-1-overexpressing human umbilical vein endothelial cells is similarly inhibited by angiotensin II, except that inhibition of 43.06% is achieved using only 10 nM angiotensin II
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the DNA-binding ability of NF-kappaB in the Ape1/Ref-1 expressing cells is significantly increased
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the key function is to produce a 3' OH terminus that serves as a primer for repair synthesis.
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ubiquitously expressed protein that functions as both an endonuclease in the repair of oxidatively damaged DNA and an aid in the binding of redox-sensitive transcription factors
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25-mer oligonucleotide 5'-labeled with P32 containing tetrahydrofuran as abasic site analog
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25-mer oligonucleotide 5'-labeled with P32 containing tetrahydrofuran as abasic site analog
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AP endo cleaves the Rp but not the Sp stereoisomer of DNA phosphorothioate oligomers, albeit slowly with respect to a phosphodiester substrate
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The ratio of AP endo reaction product to STM7 49mer hairpin oligomers is varied. Product formation is maximal with an 8:1 ratio of STM7 acceptor to 5' thiophosphate donor DNA and by addition of extra ATP (0.5 mM) and ligase (60 units) midreaction
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Used oligonucleotides are 54mers annealed to a complementary 18mer DNA to form the partial duplex substrates (54F-endbubble or 54F-centerbubble with 18DNA) and two 54mers annealed to create an 18-nt bubble structure (54Fendbubble or 54Fcenterbubble with 54bubble18comp). The abasic site is either centrally located (center bubble DNAs) or located at the ssDNA-dsDNA junction (end bubble DNAs). Ape1 most efficiently incised at an abasic site located centrally in the 18-nt bubble structure (54Fcenterbubble18-54bubblecomp), followed by the centrally located abasic site in the partial duplex DNA (54Fcenterbubble18-18DNA), the abasic site at an ssDNA/dsDNA junction in the bubble conformation (54Fendbubble18-54bubblecomp), and the abasic site at an ssDNA/dsDNA junction in partial duplex DNA (54Fendbubble18-18DNA)
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APE1 at low concentrations does not have any effect on 5'-Cy3-CrUAGGTAGTTATCCrUAG-Black Hole Quencher1-3' (OligoII), under similar conditions, the recombinant APE1 has no effect on fluorescently labeled or 32P-labeled DNAOligoI
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a 2'-OH on the sugar moiety is absolutely required for RNA cleavage by wild-type APE1, consistent with APE1 leaving a 3'-PO4 2? group following cleavage of RNA. the catalytic mechanisms for cleaving RNA, abasic single-stranded RNA, and abasic DNA are not identical
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APE1 adopts a partially unfolded state, which is proposed to be the redox active form of the enzyme
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DNA polymerase beta approaches the Ape1-DNA complex downstream of the incision site, displaces Ape1-DNA binding contacts including residues K227, K228, and K276, and in the process makes minimal interactions with lysine residues in the Ref1 domain, i.e. N-terminal residues 43-93
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wild-type APE1 undergoes at least four conformational transitions during the processing of abasic sites in DNA. Nonspecific interactions of APE1 with undamaged DNA can be described by a two-step kinetic scheme. APE1 molecule undergoes at least four conformational transitions, including nonspecific encounter complex formation, mutual adjustment of the enzyme and DNA substrate structures for catalysis, catalytic incision of the substrate, and release of the enzyme from its complex with the product. The C1'-hydroxyl moiety of the abasic site is required for the most effective recognition and catalysis
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APE1 promotes the removal of a TNR hairpin during BER of a base lesion in the hairpin loop region. This is accomplished by the 3'-5'-exonuclease activity of the enzyme that cleaved the upstream 3'-region exonucleolytically, resolving the double-flap intermediate and preventing TNR expansions. APE1 significantly stimulates the ligation activity of LIG I to specifically facilitate the completion of hairpin removal. This is the first evidence of APE1 preventing TNR expansions by facilitating hairpin removal
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APE1 promotes the removal of a TNR hairpin during BER of a base lesion in the hairpin loop region. This is accomplished by the 3'-5'-exonuclease activity of the enzyme that cleaved the upstream 3'-region exonucleolytically, resolving the double-flap intermediate and preventing TNR expansions. APE1 significantly stimulates the ligation activity of LIG I to specifically facilitate the completion of hairpin removal. This is the first evidence of APE1 preventing TNR expansions by facilitating hairpin removal
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in vivo, APE1 is acetylated (AcAPE1) after binding to the AP sites in chromatin and that AcAPE1 is exclusively present on chromatin throughout the cell cycle. Positive charges of acetylable lysine residues in the N-terminal domain of APE1 are essential for chromatin association. Acetylation-mediated neutralization of the positive charges of the lysine residues in the N-terminal domain of APE1 induces a conformational change; this in turn enhances the AP endonuclease activity of APE1. In the absence of APE1 acetylation, cells accumulate AP sites in the genome and show higher sensitivity to DNA-damaging agents. Positive charges of acetylable Lys residues but not their acetylation are essential for the chromatin binding of APE1
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in vivo, APE1 is acetylated (AcAPE1) after binding to the AP sites in chromatin and that AcAPE1 is exclusively present on chromatin throughout the cell cycle. Positive charges of acetylable lysine residues in the N-terminal domain of APE1 are essential for chromatin association. Acetylation-mediated neutralization of the positive charges of the lysine residues in the N-terminal domain of APE1 induces a conformational change; this in turn enhances the AP endonuclease activity of APE1. In the absence of APE1 acetylation, cells accumulate AP sites in the genome and show higher sensitivity to DNA-damaging agents. Positive charges of acetylable Lys residues but not their acetylation are essential for the chromatin binding of APE1
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The enzyme cleaves an AP site in DNA via Mg2+-dependent hydrolytic mechanism producing a 5'-deoxyribose phosphate and 3'-hydroxyl and, therefore, the interaction with AP sites via the Schiff base formation, which is characteristic of the beta-elimination mechanism, is not required for APE1 catalytic activity
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The enzyme cleaves an AP site in DNA via Mg2+-dependent hydrolytic mechanism producing a 5'-deoxyribose phosphate and 3'-hydroxyl and, therefore, the interaction with AP sites via the Schiff base formation, which is characteristic of the beta-elimination mechanism, is not required for APE1 catalytic activity
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the mechanism of catalysis of the APE1 endonuclease reaction includes nucleophilic attack by a hydroxide ion on the phosphorous atom at the 5'-side from AP site. The hydroxide ion is formed from a water molecule activated by the Asp210 residue. The transition complex is stabilized via formation of hydrogen bonds with the Asn174, Asn212, and His309/Asp283 residues. Glu96 participates in binding of one Mg2+, which coordinates the leaving O3'-group, and Asp210 and His309 coordinate a second metal ion participating in formation of a hydroxide ion from a water molecule. A transition state with the phosphorous atom is formed because of the nucleophilic attack, the destabilized P-O3' bond is cleaved, and, as a result, inversion of the phosphate configuration occurs (SN2-mechanism). Slow dissociation of the APE1-DNA complex (product) prevents accumulation of single-strand breaks in DNA. The reaction rate of this step increases with increase in Mg2+ concentration and, as a result, the catalysis itself likely becomes the limiting step. Mechanism of the P-O3' bond cleavage at the 5'-side of an AP site catalyzed by human APE1 derived from the structure of the APE1-DNA complex produced by X-ray at higher resolution, overview
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the mechanism of catalysis of the APE1 endonuclease reaction includes nucleophilic attack by a hydroxide ion on the phosphorous atom at the 5'-side from AP site. The hydroxide ion is formed from a water molecule activated by the Asp210 residue. The transition complex is stabilized via formation of hydrogen bonds with the Asn174, Asn212, and His309/Asp283 residues. Glu96 participates in binding of one Mg2+, which coordinates the leaving O3'-group, and Asp210 and His309 coordinate a second metal ion participating in formation of a hydroxide ion from a water molecule. A transition state with the phosphorous atom is formed because of the nucleophilic attack, the destabilized P-O3' bond is cleaved, and, as a result, inversion of the phosphate configuration occurs (SN2-mechanism). Slow dissociation of the APE1-DNA complex (product) prevents accumulation of single-strand breaks in DNA. The reaction rate of this step increases with increase in Mg2+ concentration and, as a result, the catalysis itself likely becomes the limiting step. Mechanism of the P-O3' bond cleavage at the 5'-side of an AP site catalyzed by human APE1 derived from the structure of the APE1-DNA complex produced by X-ray at higher resolution, overview
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a fluorophore-labelled 17-mer oligonucleotide DNA substrate is used
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a fluorophore-labelled 17-mer oligonucleotide DNA substrate is used
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analysis of enzyme activity and kinetics with DNA substrates comprising duplexes of deoxyribonucleotides with one 5'-dangling end that contain a fluorescent 2-aminopurine residue at the 1st, 2nd, 4th, or 6th position from the 3'-end of the short oligonucleotide. The impact of the 3'-end nucleotide, which contains mismatched, undamaged bases or modified bases as well as an abasic site or phosphate group, on the efficiency of 3'-5'-exonuclease activity is determined. The rate-limiting step of 3'-nucleotide removal by APE1 in the 3'-5'-exonuclease process is the release of the detached nucleotide from the enzyme's active site. Exonuclease activity of APE1 is effective toward duplexes containing gaps or 5'-dangling ends. For the kinetic analysis of the 3'-5'-exonuclease reaction, the duplexes of 15 and 28 nucleotides (nt) with a 5'-dangling end served as model DNA substrates
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analysis of enzyme activity and kinetics with DNA substrates comprising duplexes of deoxyribonucleotides with one 5'-dangling end that contain a fluorescent 2-aminopurine residue at the 1st, 2nd, 4th, or 6th position from the 3'-end of the short oligonucleotide. The impact of the 3'-end nucleotide, which contains mismatched, undamaged bases or modified bases as well as an abasic site or phosphate group, on the efficiency of 3'-5'-exonuclease activity is determined. The rate-limiting step of 3'-nucleotide removal by APE1 in the 3'-5'-exonuclease process is the release of the detached nucleotide from the enzyme's active site. Exonuclease activity of APE1 is effective toward duplexes containing gaps or 5'-dangling ends. For the kinetic analysis of the 3'-5'-exonuclease reaction, the duplexes of 15 and 28 nucleotides (nt) with a 5'-dangling end served as model DNA substrates
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APE1 cleaved AP sites in the structure of DNA/RNAx02hybrid (DNA strand), singlex02stranded RNA, single-stranded DNA, and double-stranded regions of pseudo-triplex DNA-RNA complexes modeling replication and transcription intermediates. APE1 exhibits endonuclease activity during hydrolysis of an AP site on a single-stranded DNA. The activity on the single-stranded DNA is 20fold lower than on double-stranded DNA. As in the case of double-stranded DNA, endonuclease activity of APE1 depended on the presence of magnesium ions. the cleavage of single-stranded DNA with an AP site does not depend on the presence of DNA glycosylases, and it is not inhibited by the reaction product. Complexes of APE1 with double-stranded DNA containing an tetrahydrofuran residue in the center of a non-cleaved strand are not detected
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APE1 cleaved AP sites in the structure of DNA/RNAx02hybrid (DNA strand), singlex02stranded RNA, single-stranded DNA, and double-stranded regions of pseudo-triplex DNA-RNA complexes modeling replication and transcription intermediates. APE1 exhibits endonuclease activity during hydrolysis of an AP site on a single-stranded DNA. The activity on the single-stranded DNA is 20fold lower than on double-stranded DNA. As in the case of double-stranded DNA, endonuclease activity of APE1 depended on the presence of magnesium ions. the cleavage of single-stranded DNA with an AP site does not depend on the presence of DNA glycosylases, and it is not inhibited by the reaction product. Complexes of APE1 with double-stranded DNA containing an tetrahydrofuran residue in the center of a non-cleaved strand are not detected
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APE1 the base excision DNA repair system catalyzes the hydrolysis of the phosphodiester bond on the 5'-side of an apurinic/apyrimidinic site (AP-site) to give the 5'-phosphate and 3'-hydroxyl group. APE1 exhibits also 3'-5'-exonuclease activity albeit less pronounced compared to its endonuclease activity
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APE1 the base excision DNA repair system catalyzes the hydrolysis of the phosphodiester bond on the 5'-side of an apurinic/apyrimidinic site (AP-site) to give the 5'-phosphate and 3'-hydroxyl group. APE1 exhibits also 3'-5'-exonuclease activity albeit less pronounced compared to its endonuclease activity
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diverse BS-AP DNA duplexes as substrates. Purified recombinant human APE1 is capable of forming the 50 kDa-adducts with efficiency of BS-AP DNAs cross-linking to APE1 being dependent on the mutual orientation of AP sites. Identification of APE1 as a target of cross-linking to BS-AP DNA, and cross-linking of cell extract proteins from HeLa cell cell extract to AP DNA with bistranded AP sites, and AP endonuclease activity of APE1 on BS-AP DNAs, detailed overview
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diverse BS-AP DNA duplexes as substrates. Purified recombinant human APE1 is capable of forming the 50 kDa-adducts with efficiency of BS-AP DNAs cross-linking to APE1 being dependent on the mutual orientation of AP sites. Identification of APE1 as a target of cross-linking to BS-AP DNA, and cross-linking of cell extract proteins from HeLa cell cell extract to AP DNA with bistranded AP sites, and AP endonuclease activity of APE1 on BS-AP DNAs, detailed overview
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electron microscopy imaging of APE1-DNA complexes reveals oligomerization of APE1 along the DNA duplex and APE1-mediated DNA bridging followed by DNA aggregation. APE1 polymerizes on both undamaged and damaged DNA in cooperative mode. Duplex DNA and diverse oligonucleotides with single base lesion are used as substrates, stopped-flow fluorescence measurements
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electron microscopy imaging of APE1-DNA complexes reveals oligomerization of APE1 along the DNA duplex and APE1-mediated DNA bridging followed by DNA aggregation. APE1 polymerizes on both undamaged and damaged DNA in cooperative mode. Duplex DNA and diverse oligonucleotides with single base lesion are used as substrates, stopped-flow fluorescence measurements
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fluorescent-labeled oligodeoxynucleotides substrates are used, overview
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fluorescent-labeled oligodeoxynucleotides substrates are used, overview
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human apurinic/apyrimidinic (AP) endonuclease APE1 catalyses the hydrolysis of phosphodiester bonds on the 5'-side of an AP-site (in the base excision repair pathway) and of some damaged nucleotides (in the nucleotide incision repair pathway). The range of substrate specificity includes structurally unrelated damaged nucleotides. Analysis of the mechanism of broad substrate specificity of APE1, overview. Substrate specificity and substrate binding, molecular dynamics simulations. The damaged nucleotide is everted from the DNA helix and placed into the enzyme's binding pocket, which is formed by Asn174, Asn212, Asn229, Ala230, Phe266, and Trp280. Nevertheless, no damage-specific contacts are detected between these amino acid residues in the active site of the enzyme and model damaged substrates containing 1,N6-ethenoadenosine, alpha-adenosine, 5,6-dihydrouridine, or F-site. The substrate specificity of APE1 is controlled by the ability of a damaged nucleotide to flip out from the DNA duplex in response to an enzyme-induced DNA distortion
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additional information
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human apurinic/apyrimidinic (AP) endonuclease APE1 catalyses the hydrolysis of phosphodiester bonds on the 5'-side of an AP-site (in the base excision repair pathway) and of some damaged nucleotides (in the nucleotide incision repair pathway). The range of substrate specificity includes structurally unrelated damaged nucleotides. Analysis of the mechanism of broad substrate specificity of APE1, overview. Substrate specificity and substrate binding, molecular dynamics simulations. The damaged nucleotide is everted from the DNA helix and placed into the enzyme's binding pocket, which is formed by Asn174, Asn212, Asn229, Ala230, Phe266, and Trp280. Nevertheless, no damage-specific contacts are detected between these amino acid residues in the active site of the enzyme and model damaged substrates containing 1,N6-ethenoadenosine, alpha-adenosine, 5,6-dihydrouridine, or F-site. The substrate specificity of APE1 is controlled by the ability of a damaged nucleotide to flip out from the DNA duplex in response to an enzyme-induced DNA distortion
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substrates are DNA oligonucleotides which contain an 8-oxoguanine (8-oxoG). APE1 fails to directly stimulate FEN1 cleavage on a double-flap intermediate. APE1 promotes the production of the unexpanded repair product by stimulating LIG I
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substrates are DNA oligonucleotides which contain an 8-oxoguanine (8-oxoG). APE1 fails to directly stimulate FEN1 cleavage on a double-flap intermediate. APE1 promotes the production of the unexpanded repair product by stimulating LIG I
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usage of a fluorescence-based APE1 endonuclease activity assay and a plasmid DNA nicking assay
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usage of a fluorescence-based APE1 endonuclease activity assay and a plasmid DNA nicking assay
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catalytic subunit of the HSV-1 DNA polymerase (Pol) (UL30) exhibits apurinic/apyrimidinic (AP) and 5'-deoxyribose phosphate lyase activities which are integral to base excision repair and lead to DNA cleavage on the 3'-side of abasic sites and 5'-deoxyribose-5-phosphate residues that remain after cleavage by 5'-AP endonuclease. DNA lyase activity residues in the Pol domain of UL30.
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enzyme has implications on the role of BER in viral genome maintenance during lytic replication and reactivation from latency
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overexpression of AP endonuclease protects Leishmania major cells against methotrexate induced DNA fragmentation and hydrogen peroxide, key enzyme in mediating repair of abasic sites in these pathogens
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LMAP shares with APE1 the overall 3D structure and most of the catalytic groups in their active sites and can catalyze the removal of damaged nucleotides and phosphate groups from 3'-ends more efficiently than APE1
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inositol polyphosphate 5-phosphatase enzymes show high homology to AP endonucleases in regions that correspond to catalytic residues, they also share a similar mechanism of catalysis to the AP endonuclease consistent with other common functional similarities such as an absolute requirement for magnesium
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role in eliminating damaged mitochondrial genomes from the gene pool
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poly(ADP-ribose) polymerase-1 and apurinic/apyrimidinic endonuclease can interact with the same base excision repair intermediate. Competition between theses two proteins may influence their respective base excision repair related functions
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the enzyme has two distinct roles in the repair of oxidative DNA damage and in gene regulation. Absolute requirement of the enzyme for cell survival, presumably to protect against spontaneous oxidative DNA damage
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APE/Ref-1 act as tuning molecule in activated B-cells
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APE/Ref-1 affect the cell cycle by inducing nucleus-cytoplasm translocation of the cyclin-dependent kinase inhibitor p21
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APE1 binds with the highest efficiency to DNA substrate containing 5'-sugar phosphate group in the nick/gap
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APE1 exhibits 3'-phosphodiesterase, 3'-phosphatase, and 3'-5'-exonuclease activities
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APE1 is one of the candidates for the role of base excision repair (BER) pathway coordinator, which controls the whole process. APE1 participates in stimulation of activity of BER enzymes
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APE1 stimulates DNA synthesis catalyzed by DNA polymerase beta, and a human Xray repair cross-complementing group 1 protein stimulates APE1 3'-5'-exonuclease activity on 3'-recessed DNA duplex
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APEX1 is a protein involved both in the base excision repair pathways of DNA lesions and in the regulation of gene expression as a redox coactivator of different transcription factors, such as early growth response protein-1
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apurinic/apyrimidinic endonuclease 1 participates in the base excision repair of premutagenic apurinic/apyrimidinic (AP) sites
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DNA with the recessed 3'-end (DNArec) is one of the preferential substrates for APE1 3'-5'-exonuclease activity
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enzyme cleaves the DNA sugar phosphate backbone at the 5'-position in relation to the AP site, forming a nick with the hydroxyl group at the 3'-end and deoxyribose phosphate at the 5'-end
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enzyme plays a role in controlling CD40-mediated B-cell proliferation, increase in proliferation and decrease in apoptosis of primary mouse B-cells activated by CD40 cross-linking and transfected with functional APE/Ref-1 antisense oligonucleotide.
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high APE1 affinity to dsDNA
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regulation of APEX1 expression by S-adenosylmethionine, which may be one of the mechanisms of hepatocellular carconom formation
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When APE1 and DNA polymerase beta are both present, a ternary complex APE1-DNA polymerase beta-DNA is formed with the highest efficiency with DNA product of APE1 endonuclease activity and with DNA containing 5'-flap or mononucleotide-gapped DNA with 5'-p group
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APE1 most efficiently binds to DNA substrate bearing tetrahydrofuran in the middle of one of the strands (AP-dsDNA)
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for APE1 in MEF extract, efficiency of formation of protein-DNA crosslinking changes depending on the nature of 5'-group flanking the nick in DNA structure: DNAFAP-pF (100%), DNAFAP-OH (68.2%), DNAFAP-flap (54.6%), DNAFAP-gap (44.2%), DNAFAP-rec (41.3%), DNAFAP-p (41.1%)
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MtbXthA is a versatile enzyme with AP endonuclease, 3'-5' exonuclease and 3' phosphodiesterase activities. XthA forms in vivo and in vitro complexes with beta-clamp DNA, the DNA substrate mediates different interaction modes between XthA and the beta-clamp, mechanism and structure, detailed overview
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approximate ninefold augmentation in AP site incision activity at the highest concentration of beta-clamp used. Additionally, marked increase in the generation of shorter oligonucleotide fragments, smaller than 32-mer, is observed due to exonucleolytic excision of nucleotides from the 32 nucleotide oligomer
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additional information
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nicked DNA and gapped DNA are fair substrates of enzyme MtbXthA, the gap-size does not affect the excision activity, a substrate with a recessed 3'-end is preferred. DNA substrate N1 containing an abasic site analogue tetrahydrofuran (THF), is used for AP site incision activity assays. Substrate N2 that contains propanediol, tetrahydrofuran, ethane or 2' deoxyribose as the abasic residues is used for studying the effect of abasic site structure on the AP site incision activity of MtbXthA. For the preparation of the duplex DNA containing a 2' deoxyribose as abasic residue, first an oligonucleotide containing a 2' deoxyribose is prepared by enzymatic treatment of an oligonucleotide harbouring 2' deoxyuridine with uracil N-glycosylase. DNA elements have no role in the recognition of AP site containing DNA by MtbXthA. Y237 functions as a critical AP site recogniser in MtbXthA. Analysis of the 3' phosphatase and 3' phosphodiesterase activities of MtbXthA with a DNA substrate
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additional information
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nicked DNA and gapped DNA are fair substrates of enzyme MtbXthA, the gap-size does not affect the excision activity, a substrate with a recessed 3'-end is preferred. DNA substrate N1 containing an abasic site analogue tetrahydrofuran (THF), is used for AP site incision activity assays. Substrate N2 that contains propanediol, tetrahydrofuran, ethane or 2' deoxyribose as the abasic residues is used for studying the effect of abasic site structure on the AP site incision activity of MtbXthA. For the preparation of the duplex DNA containing a 2' deoxyribose as abasic residue, first an oligonucleotide containing a 2' deoxyribose is prepared by enzymatic treatment of an oligonucleotide harbouring 2' deoxyuridine with uracil N-glycosylase. DNA elements have no role in the recognition of AP site containing DNA by MtbXthA. Y237 functions as a critical AP site recogniser in MtbXthA. Analysis of the 3' phosphatase and 3' phosphodiesterase activities of MtbXthA with a DNA substrate
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additional information
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nicked DNA and gapped DNA are fair substrates of enzyme MtbXthA, the gap-size does not affect the excision activity, a substrate with a recessed 3'-end is preferred. DNA substrate N1 containing an abasic site analogue tetrahydrofuran (THF), is used for AP site incision activity assays. Substrate N2 that contains propanediol, tetrahydrofuran, ethane or 2' deoxyribose as the abasic residues is used for studying the effect of abasic site structure on the AP site incision activity of MtbXthA. For the preparation of the duplex DNA containing a 2' deoxyribose as abasic residue, first an oligonucleotide containing a 2' deoxyribose is prepared by enzymatic treatment of an oligonucleotide harbouring 2' deoxyuridine with uracil N-glycosylase. DNA elements have no role in the recognition of AP site containing DNA by MtbXthA. Y237 functions as a critical AP site recogniser in MtbXthA. Analysis of the 3' phosphatase and 3' phosphodiesterase activities of MtbXthA with a DNA substrate
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additional information
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MtbXthA is a versatile enzyme with AP endonuclease, 3'-5' exonuclease and 3' phosphodiesterase activities. XthA forms in vivo and in vitro complexes with beta-clamp DNA, the DNA substrate mediates different interaction modes between XthA and the beta-clamp, mechanism and structure, detailed overview
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additional information
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approximate ninefold augmentation in AP site incision activity at the highest concentration of beta-clamp used. Additionally, marked increase in the generation of shorter oligonucleotide fragments, smaller than 32-mer, is observed due to exonucleolytic excision of nucleotides from the 32 nucleotide oligomer
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additional information
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nicked DNA and gapped DNA are fair substrates of enzyme MtbXthA, the gap-size does not affect the excision activity, a substrate with a recessed 3'-end is preferred. DNA substrate N1 containing an abasic site analogue tetrahydrofuran (THF), is used for AP site incision activity assays. Substrate N2 that contains propanediol, tetrahydrofuran, ethane or 2' deoxyribose as the abasic residues is used for studying the effect of abasic site structure on the AP site incision activity of MtbXthA. For the preparation of the duplex DNA containing a 2' deoxyribose as abasic residue, first an oligonucleotide containing a 2' deoxyribose is prepared by enzymatic treatment of an oligonucleotide harbouring 2' deoxyuridine with uracil N-glycosylase. DNA elements have no role in the recognition of AP site containing DNA by MtbXthA. Y237 functions as a critical AP site recogniser in MtbXthA. Analysis of the 3' phosphatase and 3' phosphodiesterase activities of MtbXthA with a DNA substrate
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additional information
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MtbXthA is a versatile enzyme with AP endonuclease, 3'-5' exonuclease and 3' phosphodiesterase activities. XthA forms in vivo and in vitro complexes with beta-clamp DNA, the DNA substrate mediates different interaction modes between XthA and the beta-clamp, mechanism and structure, detailed overview
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additional information
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approximate ninefold augmentation in AP site incision activity at the highest concentration of beta-clamp used. Additionally, marked increase in the generation of shorter oligonucleotide fragments, smaller than 32-mer, is observed due to exonucleolytic excision of nucleotides from the 32 nucleotide oligomer
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additional information
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no substrate: native DNA
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no associated exonuclease activity
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no substrate: alkylated sites
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no substrate: native DNA
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no substrate: native DNA
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inactive on reduced AP sites
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an increase of APE/Ref-1 mRNA levels in the caudal region of spinal cord strongly correlates with DNA damage after traumatic spinal cord injury
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increase in phosphorylation of p53 after a decrease in Ape1 levels in sensory neuronal cultures
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multifunctional protein involved in both the repair of oxidative and alkylating DNA damage and the regulation of gene expression
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overexpressing wild-type Ape1 attentuates all the toxic effects of cisplatin in cells containing normal endogenous levels of Ape1 and in cells with reduced Ape1 levels after Ape1siRNA treatment
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reducing expression of Ape1 in neuronal cultures using small interfering RNA enhances cisplatin-induced cell killing, apoptosis, ROS generation and cisplatin-induced reduction in iCGRP release
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APE1 at low concentrations does not have any effect on 5'-Cy3-CrUAGGTAGTTATCCrUAG-Black Hole Quencher1-3' (OligoII), under similar conditions, the recombinant APE1 has no effect on fluorescently labeled or 32P-labeled DNAOligoI
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enzyme also has DNA N-glycosylase activity
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additional information
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ntg1 possesses N-glycosylase/AP lyase activity that allows recognition and repair of oxidative base damage (primarily of pyrimidines) as well as abasic sites
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additional information
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ntg2 possesses N-glycosylase/AP lyase activity that allows recognition and repair of oxidative base damage (primarily of pyrimidines) as well as abasic sites
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additional information
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the nucleotide incision repair (NIR) recruiting Saccharomyces cerevisiae Apn1 proceeds via multistep rearrangements of the complex of Apn1 with a DHU-containing DNA substrate and results in the incised product of the reaction
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additional information
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substrate oligodeoxyribonucleotides (ODNs) are synthesized and purified, a fluorescent 2-aminopurine (2-aPu) probe is located either on the 5'- or 3'-side of an abasic site. Cleavage of substrates AP(2-aPu) and F(2-aPu) in several stages (F is tetrahydrofuran) by wild-type and mutant H83A enzymes, overview
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additional information
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substrate oligodeoxyribonucleotides (ODNs) are synthesized and purified, a fluorescent 2-aminopurine (2-aPu) probe is located either on the 5'- or 3'-side of an abasic site. Cleavage of substrates AP(2-aPu) and F(2-aPu) in several stages (F is tetrahydrofuran) by wild-type and mutant H83A enzymes, overview
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additional information
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substrate oligodeoxyribonucleotides (ODNs) are synthesized with a fluorescent 2-aminopurine (2-aPu) probe located either on the 5'- or 3'-side of an abasic site. Cleavage of substrates AP(2-aPu) and F(2-aPu) (F = tetrahydrofuran) in presence of Zn2+ and Mg2+ by wild-type and mutant H83A enzymes, overview. Molecular dynamics simulations elucidates the structural features of complexes of the enzyme with DHU-containing DNAs. The DNA substrate structure affects nucleotide incision repair (NIR) catalysis. Location of the 2-aPu residue near DHU decreases the efficacy of NIR activity of the WT enzyme and of H83A Apn1: nucleotide incision repair (NIR) activity of both enzymes decreases in the following descending order of substrates: DHU, DHU(2-aPu), and (2-aPu)DHU. Apn1 cannot incise the (2-aPu)DHU duplex because of the spatial structure of the (2-aPu)DHU-Apn1 complex, which is probably significantly distorted in the vicinity of the active site because two noncanonical base pairs are placed in close proximity to each other, the access of catalytically active amino acid residues and Zn2+ ions to the 5'-phosphodiester bond to be incised (located between the 2-aPu and DHU residues) might be blocked
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additional information
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substrate oligodeoxyribonucleotides (ODNs) are synthesized and purified, a fluorescent 2-aminopurine (2-aPu) probe is located either on the 5'- or 3'-side of an abasic site. Cleavage of substrates AP(2-aPu) and F(2-aPu) in several stages (F is tetrahydrofuran) by wild-type and mutant H83A enzymes, overview
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additional information
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the nucleotide incision repair (NIR) recruiting Saccharomyces cerevisiae Apn1 proceeds via multistep rearrangements of the complex of Apn1 with a DHU-containing DNA substrate and results in the incised product of the reaction
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additional information
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substrate oligodeoxyribonucleotides (ODNs) are synthesized with a fluorescent 2-aminopurine (2-aPu) probe located either on the 5'- or 3'-side of an abasic site. Cleavage of substrates AP(2-aPu) and F(2-aPu) (F = tetrahydrofuran) in presence of Zn2+ and Mg2+ by wild-type and mutant H83A enzymes, overview. Molecular dynamics simulations elucidates the structural features of complexes of the enzyme with DHU-containing DNAs. The DNA substrate structure affects nucleotide incision repair (NIR) catalysis. Location of the 2-aPu residue near DHU decreases the efficacy of NIR activity of the WT enzyme and of H83A Apn1: nucleotide incision repair (NIR) activity of both enzymes decreases in the following descending order of substrates: DHU, DHU(2-aPu), and (2-aPu)DHU. Apn1 cannot incise the (2-aPu)DHU duplex because of the spatial structure of the (2-aPu)DHU-Apn1 complex, which is probably significantly distorted in the vicinity of the active site because two noncanonical base pairs are placed in close proximity to each other, the access of catalytically active amino acid residues and Zn2+ ions to the 5'-phosphodiester bond to be incised (located between the 2-aPu and DHU residues) might be blocked
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additional information
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tetrahydrofuran-containing DNA substrates are used
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additional information
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tetrahydrofuran-containing DNA substrates are used
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additional information
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tetrahydrofuran-containing DNA substrates are used
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Tequatrovirus T4
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Tequatrovirus T4
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bacteriophage T4 endonuclease V and Escherichia coli endonuclease II catalyze N-glycosylase and 3'-abasic endonuclease reaction, beta-elimination reaction
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additional information
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enzyme displays AP endonuclease, 3'-repair phosphodiesterase, 3'-phosphatase and 3'-5' exonuclease activities. Enzyme removes 3'-blocking sugar-phosphate and 3'-phosphate groups with good efficiency but possesses a very weak AP endonuclease activity as compared to the human homologue APE1
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