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3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
3'-end 3'-dAMP-labeled 7,8-dihydro-8-oxoguanine-cytosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled alpha-anomeric 2'-deoxyadenosine-thymidine duplex + H2O
?
low efficiency
-
-
?
3'-end 3'-dAMP-labeled tetrahydrofuran-T duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled uracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled urea-thymidine duplex + H2O
?
-
-
-
?
3'-end-labeled dsDNA + H2O
?
-
-
-
-
?
3'-sticky-ended double-strand DNA + H2O
3'-blunt-ended double-strand DNA + nucleoside 5'-monophosphate
-
-
-
?
42mer double stranded DNA containing mismatches + H2O
?
the enzyme has a strong capacity for degrading double stranded DNA
-
-
?
5 mC-G duplex + H2O
?
-
-
-
?
5 ohmC-G duplex + H2O
?
-
-
-
?
5'-end-labeled dsDNA + H2O
?
-
-
-
-
?
5'-fluorescein-TTTTTTTTTTTTTTTTTTTTTTTTT-3' + H2O
?
5'-strand DNA + H2O
?
-
-
-
-
?
6-FAM-labeled double stranded DNA containing mismatches + H2O
?
-
-
-
-
?
6-FAM-labeled RNA-DNA hairpin containing mismatches + H2O
?
-
-
-
-
?
biotinylated single-stranded 56mer polynucleotide + H2O
?
-
3'-fluorescent-labeled substrate attached to streptavidin-coated reaction microspheres via a biotin linker
-
-
?
DNA containing double Holliday junctions + H2O
?
-
-
-
?
DNA containing mismatches + H2O
?
double stranded DNA containing mismatches + H2O
?
forked and nicked dsDNA containing mismatches + H2O
?
the enzyme preferentially cleaves one nucleotide inwards in a double stranded region of a forked and nicked DNA flap substrates
-
-
?
gapped DNA containing mismatches + H2O
?
-
-
-
?
mismatched DNA + H2O
?
-
the enzyme shows 5' to 3' exonuclease activity
-
-
?
nicked circular single stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches
?
nicked DNA containing mismatches + H2O
?
nicked double stranded DNA containing mismatches + H2O
?
-
-
-
?
oligonucleotide (polydA)4 + H2O
?
-
-
-
-
?
oligonucleotide (polydT)(polydA)(polydT)(polydA) + H2O
?
-
-
-
-
?
pdTpS-dApdTpS-dA + H2O
?
-
catalyzes the hydrolysis of chiral phosphothioate diesters with inversion of configuration at phosphorus
-
?
single-stranded DNA + H2O
?
single-stranded methylphosphonate 13-oligodeoxythymidylate + H2O
single-stranded methylphosphonate 13-oligodeoxythymidylate + thymidine 5'-monophosphate
-
-
degradation of methylphosphonate 13-(dT)16-mers from 15-mers to 6-mers, mainly yielded to 9-mers
?
single-stranded oligodeoxyadenylate + H2O
single-stranded oligodeoxyadenylate + adenosine 5'-monophosphate
single-stranded oligodeoxycytidylate + H2O
single-stranded oligodeoxycytidylate + cytidyl 5'-monophosphate
-
-
degradation of p(dC) polymers to products from 10-mers to 6-mers, mainly degraded to 8-mers
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
single-stranded oligodeoxythymidylate + H2O
single-stranded oligodeoxythymidylate + thymidine 5'-monophosphate
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
ssDNA 40 mer + H2O
?
-
-
-
?
ssDNA 50 mer + H2O
?
-
-
-
?
additional information
?
-
3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
-
-
-
?
5'-fluorescein-TTTTTTTTTTTTTTTTTTTTTTTTT-3' + H2O
?
-
-
-
-
?
5'-fluorescein-TTTTTTTTTTTTTTTTTTTTTTTTT-3' + H2O
?
-
-
-
-
?
damaged DNA + H2O
?
-
requirement of the Mre11 complex and exonuclease 1, playing overlapping roles, for activation of the Mec1 signaling pathway, Mre11 and Exo1 collaborate in producing long single-stranded DNA tails at double-strand breaks of DNA and promote Mec1 association with the double-strand break, Mre11 and Exo1 contribute to the activation of the replication checkpoint pathway, modeling of complex activity
-
-
?
damaged DNA + H2O
?
-
the enzyme possesses 5' to 3' exonuclease activity and acts in the Mre11 complex producing long single-stranded DNA tails at double-strand breaks of DNA
-
-
?
DNA containing mismatches + H2O
?
-
the enzyme is involved in mismatch repair and participates directly in somatic hypermutation and class-switch recombination
-
-
?
DNA containing mismatches + H2O
?
-
the enzyme is involved in mismatch repair
-
-
?
double stranded DNA containing mismatches + H2O
?
-
-
-
?
double stranded DNA containing mismatches + H2O
?
-
-
-
?
dsDNA + H2O
?
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
-
-
?
dsDNA + H2O
?
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
-
-
?
nicked DNA containing mismatches
?
-
the enzyme is part of the mismatch repair machinery, MMR, the replication factors PCNA and RFC, and Ku70/80 modulate the directionality of the enzyme-mediated excision in DNA mismatch repair, complex components and reaction process, overview
-
-
?
nicked DNA containing mismatches
?
-
the enzyme is DNA single-strand-specific, replication factors PCNA and RFC determine the enzyme reaction direction of 3' to 5' of EXOI, while WRN is modulated by Ku70/80, mechanism
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
single-stranded DNA + H2O
?
-
-
-
-
?
single-stranded DNA + H2O
?
-
the enzyme continuously degrades its substrate so that the DNA does not extend on both sides of the groove
-
?
single-stranded DNA + H2O
?
3'-5' exonuclease activity, degrades both single-stranded DNA and double-stranded DNA at similar rates
-
-
?
single-stranded DNA + H2O
?
3'-5' exonuclease activity, degrades both single-stranded DNA and double-stranded DNA at similar rates
-
-
?
single-stranded oligodeoxyadenylate + H2O
single-stranded oligodeoxyadenylate + adenosine 5'-monophosphate
-
-
mainly degraded to 9-mers
?
single-stranded oligodeoxyadenylate + H2O
single-stranded oligodeoxyadenylate + adenosine 5'-monophosphate
-
(dA)16-mers
degradation of (dA)16-mers from 15-mers to 6-mers, mainly degraded to 9-mers
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
degradation of p(dNT)18-mers from 10-mers to 7-mers
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
nucleic acid binding requires two distinct recognition sites in oligodeoxyribonucleotides
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
nucleic acid binding requires two distinct recognition sites in oligodeoxyribonucleotides
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
E. coli exonuclease I, III and V are required for stable maintenance of ColE1-related plasmids
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
inactivation of exonuclease I diverts most of plasmid replication activity from circular monomer production to synthesis of linear multimers
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
implicated in DNA repair and recombination pathways
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
quadruplex-forming and a non-quadruplex-forming oligomer as substrates.The formation of quadruplex in the oligomer inhibits its hydrolysis and quadruplex stabilization enhances the inhibition
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
excises the DNA at every two nucleotides from the 3' to 5' direction. The enzyme needs to grasp a 46 nt-long DNA strand to express its nucleolytic activity. The homo dT 30 nt-long homooligomer is the most preferable substrate for PfuExo I
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
the single-stranded DNA substrate is more sensitive than the double stranded substrate. The polymerase and exonuclease domains in the family B DNA polymerases are functionally interdependent
-
-
?
single-stranded oligodeoxythymidylate + H2O
single-stranded oligodeoxythymidylate + thymidine 5'-monophosphate
-
-
mainly degraded to 9-mers
?
single-stranded oligodeoxythymidylate + H2O
single-stranded oligodeoxythymidylate + thymidine 5'-monophosphate
-
(dT)16-mers
degradation of (dT)16-mers from 15-mers to 4-mers, mainly degraded to 9-mers
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
ssDNA + H2O
?
-
-
-
?
ssDNA + H2O
?
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
-
-
?
ssDNA + H2O
?
the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA
-
-
?
ssDNA + H2O
?
TTHB178 possesses 3'5'-ssExo activity that degrades ssDNAs containing deaminated and methylated bases, but not ssDNA containing oxidized bases or abasic sites. The enzyme functions in various DNA repair systems in cooperation with or independently of RecJ
-
-
?
ssDNA + H2O
?
TTHB178 possesses 3'5'-ssExo activity that degrades ssDNAs containing deaminated and methylated bases, but not ssDNA containing oxidized bases or abasic sites. The enzyme functions in various DNA repair systems in cooperation with or independently of RecJ
-
-
?
ssDNA 10 mer + H2O
?
-
-
-
?
ssDNA 10 mer + H2O
?
-
-
-
?
ssDNA 21 mer + H2O
?
-
-
-
?
ssDNA 21 mer + H2O
?
-
-
-
?
ssDNA 28 mer + H2O
?
-
-
-
?
ssDNA 28 mer + H2O
?
-
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair machinery, MMR, the replication factors PCNA and RFC modulate the directionality of the enzyme-mediated excision in DNA mismatch repair, complex components and reaction process, overview
-
-
?
additional information
?
-
-
the enzyme is DNA single-strand-specific
-
-
?
additional information
?
-
-
role for the single-stranded exonuclease in guarding the genome against mutagenesis by removing excess single-stranded DNA that, if left, leads to SOS induction and PolIV-dependent mutagenesis
-
-
?
additional information
?
-
ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance
-
-
?
additional information
?
-
-
ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance
-
-
?
additional information
?
-
-
self-assembling peptide EAK-oligodeoxynucleotide aggregates generated with EAK16IV at pH 4 are not degraded by exonuclease I even after 90 min. Fl-dC16-Rh complexed with EAK16IV at pH 4 shows significant nuclease resistance against exonuclease I. Aggregates prepared with EAK16IV and Fl-dC16-Rh at pH 4 protect Fl-dC16-Rh against nuclease degradation even after being incubated at pH 9.5 for 2 h. Centrifuging the EAK16IV-oligodeoxynucleotide solution immediately after sample preparation results in the loss of this nuclease protection. If the solution of EAK-oligodeoxynucleotide aggregates is centrifuged 24 h after sample preparation, the nuclease protection afforded by the EAK16IVoligodeoxynucleotide aggregates to the oligodeoxynucleotide is maintained even after being subject to a 10fold dilution and up to 4 rounds of centrifugation over 4 days
-
-
?
additional information
?
-
exonuclease I digests single-stranded DNA in the 3'-5' direction in a highly processive manner. The interactions at the anchor site, which involve all three domains of the enzyme protein and three consecutive nucleotides of the ssDNA
-
-
?
additional information
?
-
-
exonuclease I digests single-stranded DNA in the 3'-5' direction in a highly processive manner. The interactions at the anchor site, which involve all three domains of the enzyme protein and three consecutive nucleotides of the ssDNA
-
-
?
additional information
?
-
-
the enzyme is involved in repair of DNA which is damaged by UV radiation, the constitutive enzyme is phosphorylated and rapidly degraded upon arrest of DNA replication in S phase via the ubiquitin-proteasome pathway, regulation, overview
-
-
?
additional information
?
-
-
robust cleavage of transcribed G-rich DNA sequences with potential to form G loops and G4 DNA. Predicted immunoglobulin switch recombination intermediates are substrates for both exonucleolytic and 5' flap endonucleolytic cleavage
-
-
?
additional information
?
-
-
endogenous hEXO1 interacts with XPA
-
-
?
additional information
?
-
-
hEXO1 does not exhibit endonuclease activity on 5'-flaps bearing structures formed by CTG or CGG repeats, although it can excise these substrates. hEXO1 is not affected by the stem-loops formed by CTG repeats interrupting duplex regions adjacent to 5'-flaps, but the enzymes is inhibited by G4 structures formed by CGG repeats in analogous positions
-
-
?
additional information
?
-
-
a radiolabelled DNA oligonucleotide substrate or a linearized plasmid both containing 3'-overhangs are the preferred substrate for EXO1 in vitro. Pre-incubation of CtIP with either blunt-ended or 5'-overhang substrates facilitated processing by EXO1, which does not occur when the proteins are added in the reverse order
-
-
?
additional information
?
-
binding between PCNA and hEXO1 peptides p22 (aa 783-804) and p16 (aa 498-513) and isothermal titration calorimetry, overview
-
-
?
additional information
?
-
-
binding between PCNA and hEXO1 peptides p22 (aa 783-804) and p16 (aa 498-513) and isothermal titration calorimetry, overview
-
-
?
additional information
?
-
-
hEXO1 exhibits both flap endonucleolytic cleavage activity and exonucleolytic activity on the substrates carrying a duplex region or a duplex region interrupted by a (CTG)8 repeat, but not on the substrate in which a (CGG)6 repeat interrupted the duplex
-
-
?
additional information
?
-
substrate is radiolabeled 5' recessed DNA, interactions between the hExo1 protein and DNA substrate, overview
-
-
?
additional information
?
-
-
substrate is radiolabeled 5' recessed DNA, interactions between the hExo1 protein and DNA substrate, overview
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
the enzyme has 5'->3' exonuclease activity, as well as 5' structure specific DNA endonuclease activity and 5'->3' RNase H activity
-
-
?
additional information
?
-
-
the enzyme has 5'->3' exonuclease activity, as well as 5' structure specific DNA endonuclease activity and 5'->3' RNase H activity
-
-
?
additional information
?
-
the enzyme has a modest endonuclease or 5' flap activity
-
-
?
additional information
?
-
-
the enzyme has a modest endonuclease or 5' flap activity
-
-
?
additional information
?
-
-
the enzyme is associated to Mlh1 and binds to mutating V regions of DNA in BL2 cells
-
-
?
additional information
?
-
-
the enzyme is associated to Mlh1
-
-
?
additional information
?
-
-
Exo1-null mutant, is impaired in the excision step of mismatch repair. Absence of Exo1 activity diminishes/completely eliminates O6-methylguanines-induced apoptosis. Ablation of Exo1 function renders Mgmt-null cells just as resistant to alkylation-induced cytotoxicity as wild-type cells. Exo1 defect leads to a variable tissue-specific alkylation resistance phenotype. Mgmt-/- Exo1-/- mice show decreased alkylation-induced splenic atrophy, decreased alkylation-induced apoptosis in thymus and spleen tissues and decreased alkylation-induced bone marrow ablation compared with that in Mgmt-/- animals
-
-
?
additional information
?
-
-
Exo1-null mutant, is impaired in the excision step of mismatch repair. Absence of Exo1 activity diminishes/completely eliminates O6-methylguanines-induced apoptosis. Ablation of Exo1 function renders Mgmt-null cells just as resistant to alkylation-induced cytotoxicity as wild-type cells. Exo1 defect leads to a variable tissue-specific alkylation resistance phenotype. Mgmt-/- Exo1-/- mice show decreased alkylation-induced splenic atrophy, decreased alkylation-induced apoptosis in thymus and spleen tissues and decreased alkylation-induced bone marrow ablation compared with that in Mgmt-/- animals
-
-
?
additional information
?
-
OsEXO1 interacts with DNA polymerase lambda and replication protein A subunits. OsEXO1 plays an important role in both cell proliferation and UV-damaged nuclear DNA repair pathway under dark conditions
-
-
?
additional information
?
-
-
OsEXO1 interacts with DNA polymerase lambda and replication protein A subunits. OsEXO1 plays an important role in both cell proliferation and UV-damaged nuclear DNA repair pathway under dark conditions
-
-
?
additional information
?
-
no endonuclease activity with either ssDNA or dsDNA
-
-
?
additional information
?
-
-
no endonuclease activity with either ssDNA or dsDNA
-
-
?
additional information
?
-
-
the yeast two-hybrid system is employed to define regions of intermolecular interaction between small subunit DP1, large subunit DP2, and proliferating cell nuclear antigen PCNA. Intra- and intermolecular interactions between these domains are verified by using surface plasmon resonance
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair complex, Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective rad53 mutant cells by resecting newly synthesized chains and resolving the sister chromatid junctions that cause regression of collapsed forks, mechanism modeling, overview
-
-
?
additional information
?
-
-
Exo1 is involved in 5' strand resection. Sgs1 and Exo1 can act independently to remove the 5' strand. Exo1 promotes resection in the absence of Dna2. Dna2 and Exo1 nucleases process 5' strands at a DSB
-
-
?
additional information
?
-
-
yeast Exo1 interacts with human MLH1 through its Mlh1 interacting protein box (R-SK-[Y/F]-F-motif). A mutant of MLH1 targeted at site S2 (Mlh1-E682A) behaves as a hypomorphic form of Exo1. The site S2 in Mlh1 mediates Exo1 recruitment in order to optimize mismatch repair-dependent mutation avoidance
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
additional information
?
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
additional information
?
-
no activity against ssRNA and dsDNA is observed
-
-
?
additional information
?
-
-
no activity against ssRNA and dsDNA is observed
-
-
?
additional information
?
-
no activity against ssRNA and dsDNA is observed
-
-
?
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3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
3'-end 3'-dAMP-labeled 7,8-dihydro-8-oxoguanine-cytosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled alpha-anomeric 2'-deoxyadenosine-thymidine duplex + H2O
?
low efficiency
-
-
?
3'-end 3'-dAMP-labeled tetrahydrofuran-T duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled uracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled urea-thymidine duplex + H2O
?
-
-
-
?
3'-sticky-ended double-strand DNA + H2O
3'-blunt-ended double-strand DNA + nucleoside 5'-monophosphate
-
-
-
?
5 mC-G duplex + H2O
?
-
-
-
?
5 ohmC-G duplex + H2O
?
-
-
-
?
damaged DNA + H2O
?
-
requirement of the Mre11 complex and exonuclease 1, playing overlapping roles, for activation of the Mec1 signaling pathway, Mre11 and Exo1 collaborate in producing long single-stranded DNA tails at double-strand breaks of DNA and promote Mec1 association with the double-strand break, Mre11 and Exo1 contribute to the activation of the replication checkpoint pathway, modeling of complex activity
-
-
?
DNA containing double Holliday junctions + H2O
?
-
-
-
?
DNA containing mismatches + H2O
?
-
the enzyme is involved in mismatch repair and participates directly in somatic hypermutation and class-switch recombination
-
-
?
double stranded DNA containing mismatches + H2O
?
gapped DNA containing mismatches + H2O
?
-
-
-
?
nicked circular single stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches
?
-
the enzyme is part of the mismatch repair machinery, MMR, the replication factors PCNA and RFC, and Ku70/80 modulate the directionality of the enzyme-mediated excision in DNA mismatch repair, complex components and reaction process, overview
-
-
?
nicked DNA containing mismatches + H2O
?
nicked double stranded DNA containing mismatches + H2O
?
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
additional information
?
-
3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled (5R,6S)-thymine glycol-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 1,N6-ethenoadenine-thymidine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrothymine-adenosine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5,6-dihydrouracil-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
-
-
-
?
3'-end 3'-dAMP-labeled 5-hydroxycytosine-guanine duplex + H2O
?
-
-
-
?
double stranded DNA containing mismatches + H2O
?
-
-
-
?
double stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
-
?
nicked DNA containing mismatches + H2O
?
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
nucleic acid binding requires two distinct recognition sites in oligodeoxyribonucleotides
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
nucleic acid binding requires two distinct recognition sites in oligodeoxyribonucleotides
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
E. coli exonuclease I, III and V are required for stable maintenance of ColE1-related plasmids
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
inactivation of exonuclease I diverts most of plasmid replication activity from circular monomer production to synthesis of linear multimers
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
implicated in DNA repair and recombination pathways
-
?
single-stranded oligodeoxyribonucleotide + H2O
single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
single-stranded polydeoxyribonucleotide + H2O
single-stranded oligodeoxynucleotide + nucleoside 5'-monophosphate
-
-
-
?
ssDNA + H2O
?
-
-
-
?
ssDNA + H2O
?
TTHB178 possesses 3'5'-ssExo activity that degrades ssDNAs containing deaminated and methylated bases, but not ssDNA containing oxidized bases or abasic sites. The enzyme functions in various DNA repair systems in cooperation with or independently of RecJ
-
-
?
ssDNA + H2O
?
TTHB178 possesses 3'5'-ssExo activity that degrades ssDNAs containing deaminated and methylated bases, but not ssDNA containing oxidized bases or abasic sites. The enzyme functions in various DNA repair systems in cooperation with or independently of RecJ
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair machinery, MMR, the replication factors PCNA and RFC modulate the directionality of the enzyme-mediated excision in DNA mismatch repair, complex components and reaction process, overview
-
-
?
additional information
?
-
-
role for the single-stranded exonuclease in guarding the genome against mutagenesis by removing excess single-stranded DNA that, if left, leads to SOS induction and PolIV-dependent mutagenesis
-
-
?
additional information
?
-
ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance
-
-
?
additional information
?
-
-
ssDNA-binding protein stimulates ExoI by recruiting the enzyme to its substrate and provides a structural paradigm for understanding ssDNA-binding protein's organizational role in genome maintenance
-
-
?
additional information
?
-
-
the enzyme is involved in repair of DNA which is damaged by UV radiation, the constitutive enzyme is phosphorylated and rapidly degraded upon arrest of DNA replication in S phase via the ubiquitin-proteasome pathway, regulation, overview
-
-
?
additional information
?
-
-
endogenous hEXO1 interacts with XPA
-
-
?
additional information
?
-
-
hEXO1 does not exhibit endonuclease activity on 5'-flaps bearing structures formed by CTG or CGG repeats, although it can excise these substrates. hEXO1 is not affected by the stem-loops formed by CTG repeats interrupting duplex regions adjacent to 5'-flaps, but the enzymes is inhibited by G4 structures formed by CGG repeats in analogous positions
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
the enzyme has 5'->3' exonuclease activity, as well as 5' structure specific DNA endonuclease activity and 5'->3' RNase H activity
-
-
?
additional information
?
-
-
the enzyme has 5'->3' exonuclease activity, as well as 5' structure specific DNA endonuclease activity and 5'->3' RNase H activity
-
-
?
additional information
?
-
-
the enzyme is associated to Mlh1 and binds to mutating V regions of DNA in BL2 cells
-
-
?
additional information
?
-
-
Exo1-null mutant, is impaired in the excision step of mismatch repair. Absence of Exo1 activity diminishes/completely eliminates O6-methylguanines-induced apoptosis. Ablation of Exo1 function renders Mgmt-null cells just as resistant to alkylation-induced cytotoxicity as wild-type cells. Exo1 defect leads to a variable tissue-specific alkylation resistance phenotype. Mgmt-/- Exo1-/- mice show decreased alkylation-induced splenic atrophy, decreased alkylation-induced apoptosis in thymus and spleen tissues and decreased alkylation-induced bone marrow ablation compared with that in Mgmt-/- animals
-
-
?
additional information
?
-
-
Exo1-null mutant, is impaired in the excision step of mismatch repair. Absence of Exo1 activity diminishes/completely eliminates O6-methylguanines-induced apoptosis. Ablation of Exo1 function renders Mgmt-null cells just as resistant to alkylation-induced cytotoxicity as wild-type cells. Exo1 defect leads to a variable tissue-specific alkylation resistance phenotype. Mgmt-/- Exo1-/- mice show decreased alkylation-induced splenic atrophy, decreased alkylation-induced apoptosis in thymus and spleen tissues and decreased alkylation-induced bone marrow ablation compared with that in Mgmt-/- animals
-
-
?
additional information
?
-
OsEXO1 interacts with DNA polymerase lambda and replication protein A subunits. OsEXO1 plays an important role in both cell proliferation and UV-damaged nuclear DNA repair pathway under dark conditions
-
-
?
additional information
?
-
-
OsEXO1 interacts with DNA polymerase lambda and replication protein A subunits. OsEXO1 plays an important role in both cell proliferation and UV-damaged nuclear DNA repair pathway under dark conditions
-
-
?
additional information
?
-
-
the enzyme is part of the mismatch repair complex, Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective rad53 mutant cells by resecting newly synthesized chains and resolving the sister chromatid junctions that cause regression of collapsed forks, mechanism modeling, overview
-
-
?
additional information
?
-
-
Exo1 is involved in 5' strand resection. Sgs1 and Exo1 can act independently to remove the 5' strand. Exo1 promotes resection in the absence of Dna2. Dna2 and Exo1 nucleases process 5' strands at a DSB
-
-
?
additional information
?
-
-
yeast Exo1 interacts with human MLH1 through its Mlh1 interacting protein box (R-SK-[Y/F]-F-motif). A mutant of MLH1 targeted at site S2 (Mlh1-E682A) behaves as a hypomorphic form of Exo1. The site S2 in Mlh1 mediates Exo1 recruitment in order to optimize mismatch repair-dependent mutation avoidance
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
additional information
?
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
-
Ku restricts the access of the enzyme to DNA ends. DNA with ends occluded by the DNA end-joining factor Ku70-Ku80 is a suitable substrate for long-range 5'->3' resection when a nick is introduced at a locale proximal to one of the Ku-bound DNA ends
-
-
?
additional information
?
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
the enzyme has 5'-3' double stranded DNA exonuclease and flap endonuclease activities. The enzyme functions to excise the daughter strand after mispair recognition. Additionally, the enzyme functions in end resection during recombination. However, it is not absolutely required for end resection during recombination in vivo
-
-
?
additional information
?
-
-
Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
-
-
?
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0.0043 - 1
single-stranded DNA-binding protein
-
0.0043
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WDFDDDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0052
single-stranded DNA-binding protein
Escherichia coli
-
wild type peptide inhibitor, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0067
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with neutralizing modification WMDFDADIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0085
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with neutralizing modification WMDFADDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0093
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with neutralizing modification WMDFDDAIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0116
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with neutralizing modification WMAFDDDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0121
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WFDDDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0253
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WDDDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0335
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WDDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0529
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with C-terminal modification/truncation WMDFDDDISF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.0791
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WDIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.169
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with neutralizing modification WMAFAAAIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.252
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with N-terminal truncation WIPF, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
0.382
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with C-terminal modification/truncation WMDFDDDIPY, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
1
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with C-terminal modification/truncation WMDFDDD, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
1
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with C-terminal modification/truncation WMDFDDDI, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
1
single-stranded DNA-binding protein
Escherichia coli
-
peptide inhibitor with C-terminal modification/truncation WMDFDDDIP, at 22°C in 20 mM Tris-HCl buffer, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 1 mM 2-mercaptoethanol, 0.1 g/l bovine serum albumin, 4% (v/v) glycerol, 1% (v/v) dimethyl sulfoxide
-
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metabolism
exonuclease 1 is a multifunctional 5'->3' exonuclease and a DNA structure-specific DNA endonuclease
evolution
-
exonuclease 1 is highly conserved from yeast to human
evolution
the enzyme is a member of the RAD2 nuclease family
malfunction
-
enzyme-deficient exo1DELTA yeast cells repairing plasmids with 5'-extensions can produce repair junction with templated insertions. Exo1D mutants have a reduced median size of deletions when joining DNA with blunt ends, and exo1D pol4D mutants repair blunt ends with a very low frequency of deletions, phenotypes, overview
malfunction
-
in nonreplicating cells, depletion or downregulation of hEXO1 reduces unscheduled DNA synthesis after UV irradiation, prevents ubiquitylation of histone H2A, and impairs activation of the checkpoint signal transduction cascade in response to UV damage
malfunction
-
nearly all double-strand breaks are converted to chromosome breaks in cells lacking both exonuclease 1 activity and RAD50/MRE11/XRS2, MRX, complex
malfunction
-
on exposure to camptothecin, depletion of EXO1 in CtIP-deficient cells increases the frequency of DNA-PK-dependent radial chromosome formation
malfunction
a defect of the enzyme is associated with different types of cancers, including Lynch Syndrome, breast, ovarian, lung, pancreatic, and gastric tract cancer
malfunction
enzyme mutations correlate with increased susceptibility to some cancers
malfunction
-
enzyme-deficient exo1DELTA yeast cells repairing plasmids with 5'-extensions can produce repair junction with templated insertions. Exo1D mutants have a reduced median size of deletions when joining DNA with blunt ends, and exo1D pol4D mutants repair blunt ends with a very low frequency of deletions, phenotypes, overview
-
physiological function
-
DNA processing or resection carried out in the presence of Exo1 is efficient at preventing the double-strand break to chromosome break transition and that the exonuclease activity associated with exonuclease 1 plays a major role. Some feature of exonuclease processing or resection at a double-strand break is critical for maintaining broken chromosome ends in close proximity, additional role for Exo1 of maintaining chromosome continuity upon introduction of a double-strand break
physiological function
-
end resection of DNA, which is essential for the repair of DNA double-strand breaks by homologous recombination, relies first on the partnership between MRE11-RAD50-NBS1 and CtIP, followed by a processive step involving helicases and exonucleases such as exonuclease 1. Localization of EXO1 to double-strand breaks depends on both CtIP and MRE11-RAD50-NBS1. CtIP and EXO1 cooperate to prevent non-homologous end-joining
physiological function
-
Exo1 acts at a late stage in end-processing during non-homologous end-joining, NHEJ. Exo1 can reverse nucleotide additions occurring due to polymerization, and may also be important for processing ends to expose microhomologies needed for NHEJ. Acurate joining is controlled at two steps, a first step that blocks mdification of DNA ends, which requires Tdp1, and a second step that occurs after synapsis that requires Exo1, overview
physiological function
-
EXO1 can eliminate structures formed by trinucleotide repeats in the course of DNA replication
physiological function
-
exonuclease 1 is implicated in numerous DNA metabolic pathways, including repair, recombination, replication, and telomere maintenance. Key role for hEXO1 in the UV-induced DNA damage response linking NER to checkpoint activation in human cells. hEXO1 accumulation requires XPF-dependent processing of UV-induced lesions and is enhanced by inhibition of DNA repair synthesis
physiological function
human exonuclease 1 is a multifunctional protein that plays roles in DNA metabolism, including replication, recombination and repair, substantiated by its interactions with proliferating cell nuclear antigen, DNA helicases BLM and WRN, and several DNA mismatch repair proteins
physiological function
human exonuclease 1 plays important roles in DNA repair and recombination processes that maintain genomic integrity, model of 5' exonuclease activity in human DNA mismatch repair, overview. Analysis of the mechanism by which this 5' structure-specific exo- and endonuclease family, including Exo1, recognizes and processes diverse DNA structures, conformational control of a mobile region in the catalytic site suggests a mechanism for allosteric regulation by binding to protein partners, overview
physiological function
-
in addition to performing a variety of functions during mitotic growth, Exo1 is also important for the production of crossovers during meiosis, the nuclease activity of exonuclease I is essential for normal 5'-3' resection at the Spo11-dependent HIS4 hotspot in otherwise wild-type cells. This same activity is also required for normal levels of gene conversion at the locus. Exo1 also plays a nuclease-independent role in crossover promotion
physiological function
in view of the strong exonuclease activity of Sso polB1 on matched dsDNA, its is suggested that Sulfolobus solfataricus may have evolved mechanisms to regulate the exonuclease/polymerase ratio of the enzyme, thereby reducing the cost of proofreading at high temperature
physiological function
-
the enzyme is involved in a Thermococcales-specific DNA-repair pathway
physiological function
the enzyme contributes to checkpoint progression and to several DNA repair pathways involved in reducing DNA replication stress, for example, in mismatch repair, translesion DNA synthesis, nucleotide excision repair, double-strand break repair, and checkpoint activation to restart stalled DNA forks
physiological function
the enzyme plays roles in telomere maintenance, DNA replication, DNA mismatch repair and DNA double-stranded break repair and contributes to meiosis, immunoglobulin maturation, and micro-mediated end-joining
physiological function
-
in view of the strong exonuclease activity of Sso polB1 on matched dsDNA, its is suggested that Sulfolobus solfataricus may have evolved mechanisms to regulate the exonuclease/polymerase ratio of the enzyme, thereby reducing the cost of proofreading at high temperature
-
physiological function
-
in addition to performing a variety of functions during mitotic growth, Exo1 is also important for the production of crossovers during meiosis, the nuclease activity of exonuclease I is essential for normal 5'-3' resection at the Spo11-dependent HIS4 hotspot in otherwise wild-type cells. This same activity is also required for normal levels of gene conversion at the locus. Exo1 also plays a nuclease-independent role in crossover promotion
-
physiological function
-
Exo1 acts at a late stage in end-processing during non-homologous end-joining, NHEJ. Exo1 can reverse nucleotide additions occurring due to polymerization, and may also be important for processing ends to expose microhomologies needed for NHEJ. Acurate joining is controlled at two steps, a first step that blocks mdification of DNA ends, which requires Tdp1, and a second step that occurs after synapsis that requires Exo1, overview
-
physiological function
-
the enzyme is involved in a Thermococcales-specific DNA-repair pathway
-
additional information
-
comparison of exonuclease 1, EXO1, and Flap endonuclease 1, FEN1, activities on G4 DNA substrates, hFEN1, but not hEXO1, cleaves 59 telomeric G4 DNA, overview. Telomeres are composed of G-rich repeats that readily form G4 DNA. human EXO1 and FEN1 exhibit distinct activities on G4 DNA substrates representative of intermediates in immunoglobulin class switch recombination, distinct telomeric phenotypes caused by EXO1 and FEN1 deficiencies, overview
additional information
mapping of region on hEXO1 required for recruitment to DNA double strand breaks, mechanism of hEXO1 recruitment, overview
additional information
-
mapping of region on hEXO1 required for recruitment to DNA double strand breaks, mechanism of hEXO1 recruitment, overview
additional information
structures of hExo1 in complex with a DNA substrate, overview
additional information
-
structures of hExo1 in complex with a DNA substrate, overview
additional information
-
two-step model of DNA end resection
additional information
the enzyme crystal structure, in the absence of DNA, shows a C-shaped molecule with three domains that form a central positively charged groove. The active site is at the bottom of the groove, while an extended loop, proposed to encircle the DNA, crosses over the groove. Analysis of the active site structure of enzyme with bound ssDNA nucleotides, overview
additional information
-
the enzyme crystal structure, in the absence of DNA, shows a C-shaped molecule with three domains that form a central positively charged groove. The active site is at the bottom of the groove, while an extended loop, proposed to encircle the DNA, crosses over the groove. Analysis of the active site structure of enzyme with bound ssDNA nucleotides, overview
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D319A
does not alter the secondary structure significantly. 2-fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E150A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E318A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
K227A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
L331A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Q311A
does not alter the secondary structure significantly. Displays modest 2fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R148A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R316A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R327A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R338A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Y207A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
A153V
the mutation is associated with colorectal cancer and cancer of the small intestine
E109K
the mutation is associated with colorectal cancer
E589K
the mutation is associated with gastric cancer, lung cancer, hepatocellular carcinoma, melanoma, and glioblastoma
E670G
the mutation is associated with gastric cancer, breast cancer, oral cancer, lung cancer, melanoma, and glioblastoma
F506A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
F507A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
N279S
the mutation is associated with breast cancer and pancreatic cancer
P757L
the mutation is associated with colorectal cancer, pancreatic cancer, gastric cancer, breast cancer, oral cancer, lung cancer, and melanoma
Q154A/Y157A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
Q285A/F288A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
R723G/R723S
the mutation is associated with gastric cancer, breast cancer, oral cancer, and lung cancer
S504A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
T439M
the mutation is associated with colorectal cancer
D368A
-
the exonuclease-deficient mutant is drastically impaired for 3'-to-5' exonuclease activity, with no activity detected even at high enzyme-to-DNA substrate ratios
D405A
-
mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
D405E
-
mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
DELTAH672-S775
-
mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL717-S775
-
mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL746-S775
-
mutant protein has DNA polymerizing activity with 2.3fold higher specific activity than that of the wild-type but retains only 10% of the 3'->5' exonucleolytic activity of the wild-type
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
F447A
-
abolishes binding to human MLH1
F448A
-
abolishes binding to human MLH1
S445A
-
abolishes binding to human MLH1
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
-
D173A
-
with either mutant D173A alone or both mutant D173A and BLM, nucleolytic degradation is undetectable. It competitively inhibits Exo1-BLM-mediated resection
D173A
inactive mutant, structure in complex with Ca2+, overview
F506A/F507A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
F506A/F507A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
additional information
-
mutant lacking RecJ, ExoI, ExoVII and ExoX exonucleases abolishes normal mismatch repair in vitro but confers only a modest increase in mutation rate
additional information
-
the quadruple mutant lacking RecJ, ExoI, ExoVII and ExoX exonucleases and the triple mutant lacking RecJ, ExoI and ExoVII are characterized by sensitivity to the base analogous 2-aminopurine. The quadruple mutant displays a cold-sensitive phenotype and is unable to form colonies at 30°C on rich medium
additional information
-
in RecBCD+ cells, a mutated single-strand DNA 3'-5' exonuclease ExoI induces an increase in stationary-phase mutation. In sbcB15 cells, as in wild-type cells, these mutations partially require RecA, RecB, RecF, and expression of the LexA regulon. Absence of ExoI (DELTAxon) in wild-type or sbcC cells does not change significantly the stationary-phase mutation
additional information
analysis of single- and multiple-point mutants reveals that mutation to Ala of the three hydroxyurea-induced sites of phosphorylation partially rescues hydroxyurea-dependent degradation of hEXO1 and additionally stabilizes the protein in non-treated cells
additional information
-
analysis of single- and multiple-point mutants reveals that mutation to Ala of the three hydroxyurea-induced sites of phosphorylation partially rescues hydroxyurea-dependent degradation of hEXO1 and additionally stabilizes the protein in non-treated cells
additional information
-
various DNA damage phenotypes in response to camptothecin occur after siRNA-mediated downregulation of CtIP and EXO1
additional information
-
construction of enzyme-deficient mutant mice which show a deficient humoral response and immunoglobulin switching defects, the mutant mice show altered patterns of somatic hypermutation, overview
additional information
-
switch junction position is altered in Exo1-/- mice
additional information
generation of a mutant enzyme that is defective for the function of Exo1p in DNA mismatch repair due to disrupted interaction with Mlh1p, but still functional for post-replication repair
additional information
-
exo1DELTA but not mlh1-E682A presents significant increase in canavanin-resistant mutant events. Mlh1-R547A exo1DELTA and mlh1-E682A exo1DELTA double mutants show that mlh1-R547A synergistically interacts with exo1DELTA, yielding high canavanin-resistant forward and Hom+ reversion mutation rates, whereas mlh1-E682A does not
additional information
-
initiation of resection in exo1DELTA mutant cells is comparable to that in wild-type cells. In exo1DELTA sgs1DELTA double mutants, the Mre11-Rad50-Xrs2 complex together with Sae2 nuclease generate, in a stepwise manner, only few hundred nucleotides of ssDNA at the break, resulting in inefficient gene conversion and G2/M damage checkpoint arrest. Resection in sgs1DELTA exo1DELTA is limited to the vicinity of double-strand break ends and depends on the Mre11-Rad50-Xrs2 complex and Sae2. G2/M checkpoint arrest in response to a single double-strand break is impaired in sgs1D exo1D cells
additional information
-
sensitivity of rad53 mutants to DNA-damaging agents can be almost completely suppressed by deletion of the EXO1 gene. Deletion of EXO1 also suppresses DNA replication fork instability in rad53 mutants. Deletion of EXO1 is completely ineffective in suppressing both the sensitivity and replication fork breakdown in mec1 mutants
additional information
-
when the exo1DELTA or the exo1-D173A nuclease mutations are combined with a rad50DELTA mutation, the frequency of large budded cells with a CRB following I-SceI induction increases to 80% or 65% with HO, induction of CRBs by HO-endonuclease is also increased in an exo1DELTA mutant
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Saccharolobus solfataricus (P26811), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P26811)
brenda
Miyazono, K.I.; Tsutsumi, K.; Ishino, Y.; Tanokura, M.
Expression, high-pressure refolding, purification, crystallization and preliminary X-ray analysis of a novel single-strand-specific 3'-5' exonuclease PhoExo I from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
70
1076-1079
2014
Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428
brenda
Korada, S.K.; Johns, T.D.; Smith, C.E.; Jones, N.D.; McCabe, K.A.; Bell, C.E.
Crystal structures of Escherichia coli exonuclease I in complex with single-stranded DNA provide insights into the mechanism of processive digestion
Nucleic Acids Res.
41
5887-5897
2013
Escherichia coli (P04995), Escherichia coli
brenda
Tang, X.; Shen, Y.; Matsui, E.; Matsui, I.
Domain topology of the DNA polymerase D complex from a hyperthermophilic archaeon Pyrococcus horikoshii
Biochemistry
43
11818-11827
2004
Pyrococcus horikoshii
brenda
Redrejo-Rodriguez, M.; Vigouroux, A.; Mursalimov, A.; Grin, I.; Alili, D.; Koshenov, Z.; Akishev, Z.; Maksimenko, A.; Bissenbaev, A.; Matkarimov, B.; Saparbaev, M.; Ishchenko, A.; Morera, S.
Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA
Biochimie
128-129
20-33
2016
Bacillus subtilis (P37454), Bacillus subtilis 168 (P37454)
brenda
Keijzers, G.; Bohr, V.A.; Rasmussen, L.J.
Human exonuclease 1 (EXO1) activity characterization and its function on flap structures
Biosci. Rep.
35
e00206
2015
Homo sapiens (Q9UQ84), Homo sapiens
brenda
Keijzers, G.; Liu, D.; Rasmussen, L.
Exonuclease 1 and its versatile roles in DNA repair
Crit. Rev. Biochem. Mol. Biol.
51
440-451
2016
Homo sapiens (Q9UQ84)
-
brenda
Goellner, E.M.; Putnam, C.D.; Kolodner, R.D.
Exonuclease 1-dependent and independent mismatch repair
DNA Repair
32
24-32
2015
Saccharomyces cerevisiae (P39875), Saccharomyces cerevisiae, Homo sapiens (Q9UQ84), Homo sapiens
brenda
Keijzers, G.; Bakula, D.; Petr, M.A.; Madsen, N.G.K.; Teklu, A.; Mkrtchyan, G.; Osborne, B.; Scheibye-Knudsen, M.
Human exonuclease 1 (EXO1) regulatory functions in DNA replication with putative roles in cancer
Int. J. Mol. Sci.
20
E74
2018
Homo sapiens (Q9UQ84), Homo sapiens
brenda
Wang, W.; Daley, J.M.; Kwon, Y.; Xue, X.; Krasner, D.S.; Miller, A.S.; Nguyen, K.A.; Williamson, E.A.; Shim, E.Y.; Lee, S.E.; Hromas, R.; Sung, P.
A DNA nick at Ku-blocked double-strand break ends serves as an entry site for exonuclease 1 (Exo1) or Sgs1-Dna2 in long-range DNA end resection
J. Biol. Chem.
293
17061-17069
2018
Saccharomyces cerevisiae (P39875), Saccharomyces cerevisiae
brenda
Lawler, J.L.; Mukherjee, P.; Coen, D.M.
Herpes simplex virus 1 DNA polymerase RNase H activity acts in a 3'-to-5' direction and is dependent on the 3'-to-5' exonuclease active site
J. Virol.
92
e01813-17
2018
Human alphaherpesvirus 1
brenda