3.1.11.1: exodeoxyribonuclease I
This is an abbreviated version!
For detailed information about exodeoxyribonuclease I, go to the full flat file.
Word Map on EC 3.1.11.1
-
3.1.11.1
-
camp
-
cyclase
-
adenylate
-
monophosphate
-
agonist
-
forskolin
-
ibmx
-
cardiac
-
arterial
-
theophylline
-
pulmonary
-
rolipram
-
ventricular
-
calmodulin
-
prostaglandin
-
inotropic
-
guanosine
-
3-isobutyl-1-methylxanthine
-
milrinone
-
vasodilator
-
isoproterenol
-
klenow
-
camp-dependent
-
contractile
-
polymerases
-
adenylyl
-
sildenafil
-
isobutylmethylxanthine
-
guanylate
-
dibutyryl
-
papaverine
-
beta-adrenergic
-
erectile
-
hemodynamic
-
calmodulin-dependent
-
prostacyclin
-
rhodopsin
-
guanylyl
-
beta-adrenoceptor
-
3',5'-monophosphate
-
pentoxifylline
-
isoprenaline
-
dipyridamole
-
dntp
-
drug development
-
transducin
-
molecular biology
-
tadalafil
-
phototransduction
-
chronotropic
-
bronchodilator
-
analysis
-
dobutamine
- 3.1.11.1
- camp
- cyclase
- adenylate
- monophosphate
- agonist
- forskolin
- ibmx
- cardiac
- arterial
- theophylline
- pulmonary
- rolipram
- ventricular
- calmodulin
- prostaglandin
-
inotropic
- guanosine
- 3-isobutyl-1-methylxanthine
- milrinone
-
vasodilator
- isoproterenol
-
klenow
-
camp-dependent
-
contractile
- polymerases
-
adenylyl
- sildenafil
- isobutylmethylxanthine
-
guanylate
-
dibutyryl
- papaverine
-
beta-adrenergic
-
erectile
-
hemodynamic
-
calmodulin-dependent
- prostacyclin
- rhodopsin
-
guanylyl
-
beta-adrenoceptor
-
3',5'-monophosphate
- pentoxifylline
- isoprenaline
- dipyridamole
- dntp
- drug development
- transducin
- molecular biology
- tadalafil
-
phototransduction
-
chronotropic
-
bronchodilator
- analysis
- dobutamine
Reaction
Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =
Synonyms
3'->5'exonuclease, 3'-to-5' exonuclease, 3'5' exonuclease, 30–50 ssExo, DNA deoxyribophosphodiesterase, DNA polymerase D, DNA polymerase I, dRPase, E. coli exonuclease I, EC 3.1.4.25, Escherichia coli exonuclease I, Exo I, Exo1, EXO1b, ExoA, ExoI, exonuclease 1, exonuclease 1b, exonuclease I, exonuxlease 1, hEXO1, More, OsEXO1, PF2046, PfuExo I, PhoExo I, phosphodiesterase, Pol, Pol BI, POlB1, polD, SbcB15, single-strand DNA 3'-5' exonuclease, single-strand-specific 3'-5' exonuclease, single-stranded DNA-specific 3'-5' exonuclease I, Sso polB1, SSO0552, tthb178, WRN
ECTree
3.1.11.1 exodeoxyribonuclease IAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.1.11.1 - exodeoxyribonuclease I
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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'-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
-
-
?
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
-
-
?
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
-
-
?
mismatched DNA + H2O
?
-
the enzyme shows 5' to 3' exonuclease activity
-
-
?
nicked circular single stranded DNA containing mismatches + H2O
?
-
-
-
?
nicked double stranded DNA containing mismatches + H2O
?
-
-
-
?
pdTpS-dApdTpS-dA + H2O
?
-
catalyzes the hydrolysis of chiral phosphothioate diesters with inversion of configuration at phosphorus
-
?
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
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
?
-
-
-
-
?
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
-
-
?
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
-
-
?
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 4–6 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
?
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
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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
?
-
-
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 EAK16IV–oligodeoxynucleotide 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
?
-
-
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
?
-
-
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
?
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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
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additional information
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Exo1 possesses both 5'-3' exonuclease and 5' flap endonuclease activities
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additional information
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no activity against ssRNA and dsDNA is observed
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additional information
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no activity against ssRNA and dsDNA is observed
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
no activity against ssRNA and dsDNA is observed
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