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Information on EC 3.1.11.6 - exodeoxyribonuclease VII
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EC Tree
3.1.11.6 exodeoxyribonuclease VIISpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates
Synonyms
exonuclease vii, exovii, escherichia coli exonuclease vii, exodeoxyribonuclease vii, e. coli exonuclease vii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E. coli exonuclease VII
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endodeoxyribonuclease VII
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-
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Escherichia coli exonuclease VII
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exonuclease VII
ExoVII
nuclease, exodeoxyribo-, VII
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-
-
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XseA
exonuclease VII
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
52933-20-7
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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
polydeoxyribonucleotides + H2O
hydrolyzed single-stranded DNA
-
-
-
?
duplex DNA containing single-stranded termini + H2O
hydrolyzed single-stranded DNA
-
-
-
?
duplex DNA containing single-stranded termini + H2O
hydrolyzed single-stranded DNA
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-
-
?
single-stranded DNA + H2O
?
-
ExoVII activity is highly processive. It binds ssDNA ends and cleaves its substrate endonucleolytically, releasing oligonucleotide products of various sizes
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-
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
-
-
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no activity on circular DNA
exclusively oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no activity on circular DNA
exclusively oligonucleotides, no mononucleotide production observed
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no endonuclease activity
limit products: oligonucleotides: dimers to dodecamers
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no activity homopolymers
limit products: oligonucleotides: dimers to dodecamers
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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processive degradation
-
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
processive degradation
limit products: oligonucleotides: dimers to dodecamers
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
processive degradation
exclusively oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
processive degradation
exclusively oligonucleotides, no mononucleotide production observed
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no activity on DNA-RNA hybrid molecules
exclusively oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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no activity on DNA-RNA hybrid molecules
exclusively oligonucleotides, no mononucleotide production observed
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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single stranded DNA of at least 10-20 nucleotides are required for maximal activity
exclusively oligonucleotides, no mononucleotide production observed
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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heat-denatured DNA
exclusively oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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no activity on RNA
exclusively oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
no activity on RNA
exclusively oligonucleotides, no mononucleotide production observed
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
-
?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in methyl-directed mismatch repair system
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
possible role in methyl-directed mismatch repair system
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
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?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
-
?
thymine dimers + H2O
hydrolyzed single-stranded DNA
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possible role in repair of ultraviolet damage
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?
additional information
?
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involved in methyl-directed mismatch repair
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-
?
additional information
?
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RecBCD subunit RecD is required for initiation of homologous recombination in Escherichia coli and essential for phage lambda recombination, in contrast to exonuclease RecJ, overview
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-
?
additional information
?
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exonuclease VII can digest ssDNA from 3' ends
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?
additional information
?
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exonuclease VII cleaves msDNA, e.g. Ec78 and Ec83
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-
?
additional information
?
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exonuclease VII cleaves msDNA, e.g. Ec78 and Ec83
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?
additional information
?
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mutants lacking ExoVII are viable during all phases of the bacterial life cycle, but cannot compete with wild-type cells during long-term stationary phase incubation. Mutants lacking ExoVII are defective in DNA catabolism
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?
additional information
?
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mutants lacking ExoVII are viable during all phases of the bacterial life cycle, but cannot compete with wild-type cells during long-term stationary phase incubation. Mutants lacking ExoVII are defective in DNA catabolism
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?
additional information
?
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exonuclease VII can digest ssDNA from 3' ends
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?
additional information
?
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ExoVII is refractory to mutation, inactivation appears to be lethal. ExoVII appears to be essential for growth of Haemophilus influenzae, possibly, given its ability to process DNA flaps, indicating a requirement for the activities of this protein in replicative DNA synthesis
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-
?
additional information
?
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ExoVII is refractory to mutation, inactivation appears to be lethal. ExoVII appears to be essential for growth of Haemophilus influenzae, possibly, given its ability to process DNA flaps, indicating a requirement for the activities of this protein in replicative DNA synthesis
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-
?
additional information
?
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active site motif with two conserved aspartate residues in the large (XseA/TM1768) subunit. Residues Asp235 and Asp240 are essential for the nuclease activity
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?
additional information
?
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no significant activity on dsDNA. Active site motif with two conserved aspartate residues in the large (XseA/TM1768) subunit. Residues Asp235 and Asp240 are essential for the nuclease activity
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?
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NATURAL SUBSTRATE
NATURAL 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
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
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-
oligonucleotides
?
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
-
-
oligonucleotides
?
additional information
?
-
-
involved in methyl-directed mismatch repair
-
-
?
additional information
?
-
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RecBCD subunit RecD is required for initiation of homologous recombination in Escherichia coli and essential for phage lambda recombination, in contrast to exonuclease RecJ, overview
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?
additional information
?
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exonuclease VII can digest ssDNA from 3' ends
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?
additional information
?
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mutants lacking ExoVII are viable during all phases of the bacterial life cycle, but cannot compete with wild-type cells during long-term stationary phase incubation. Mutants lacking ExoVII are defective in DNA catabolism
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-
?
additional information
?
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mutants lacking ExoVII are viable during all phases of the bacterial life cycle, but cannot compete with wild-type cells during long-term stationary phase incubation. Mutants lacking ExoVII are defective in DNA catabolism
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-
?
additional information
?
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exonuclease VII can digest ssDNA from 3' ends
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-
?
additional information
?
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ExoVII is refractory to mutation, inactivation appears to be lethal. ExoVII appears to be essential for growth of Haemophilus influenzae, possibly, given its ability to process DNA flaps, indicating a requirement for the activities of this protein in replicative DNA synthesis
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-
?
additional information
?
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ExoVII is refractory to mutation, inactivation appears to be lethal. ExoVII appears to be essential for growth of Haemophilus influenzae, possibly, given its ability to process DNA flaps, indicating a requirement for the activities of this protein in replicative DNA synthesis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
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ExoVII activity is maximal at low salt concentrations (lower than 250 mM)
Mg2+
additional information
-
manganese, nickel, cobalt and zinc have no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
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inhibits nuclease activity at 80°C; strongly inhibits, almost complete inhibition by 50 mM
additional information
-
is not active in standard Escherichia coli ExoVII buffer. Acetate has no effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
becomes activated upon DNA damage by single-stranded DNA regions, in order to confer better opportunities for cell survival
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
exodeoxyribonuclease vii deficiency
Pyrimidine dimer excision in Escherichia coli strains deficient in exonucleases V and VII and in the 5' leads to 3' exonuclease of DNA polymerase I.
Hepatitis A
Detection of defective genomes in hepatitis A virus particles present in clinical specimens.
Herpes Simplex
Immediate-early mRNA-2 of herpes simplex viruses types 1 and 2 is unspliced: conserved sequences around the 5' and 3' termini correspond to transcription regulatory signals.
Herpes Simplex
Organization of the herpes simplex virus type 1 transcription unit encoding two early proteins with molecular weights of 140000 and 40000.
Herpes Simplex
Structures of two spliced herpes simplex virus type 1 immediate-early mRNA's which map at the junctions of the unique and reiterated regions of the virus DNA S component.
Infections
Analysis of the major transcripts encoded by the long repeat of human cytomegalovirus strain AD169.
Virus Diseases
Detection of defective genomes in hepatitis A virus particles present in clinical specimens.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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XseA/B homologs TM1768 and TM1769 show robust and maximal nuclease activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
134040, 134045, 134046, 652155, 653673, 680517, 682560, 700327, 700496, 707510, 715119, 730437, 730489
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brenda
large and small subunits, XseA and XseB
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
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ExoI- ExoVII- SbcCD- cells are sensitive to mitomycin C and 2-aminopurine. Cells lacking all three nucleases, exonuclease I, exonuclease VII, or SbcCD, are inviable without RecG. Removing RNase HI mimics the effect of removing RecG in that DrnhA cells are inviable if ExoI, ExoVII, and SbcCD are eliminated
malfunction
the absence of 3' exonucleases leads to an accumulation of 3' flaps, thereby triggering PriA-mediated overreplication of the termination area, the DnaA-independent growth is triggered by the absence of 3' exonucleases. Overreplication of the termination area in cells lacking 3' exonucleases is abolished if the chromosome is linearized
malfunction
the ExoVII- (xseB) and ExoVII- (xseA) deficient mutant strains are both inactive with msDNA. Overexpression of the large subunit is lethal, and cells harboring a plasmid encoding xseA have much lower ExoVII activity than wild-type cells. MsDNA cleavage and cell death at various subunit ratios, overview. The N-terminal domain of XseA causes cell death, and the chromosome is fragmented and condensed in the cells dying by XseA
malfunction
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ExoI- ExoVII- SbcCD- cells are sensitive to mitomycin C and 2-aminopurine. Cells lacking all three nucleases, exonuclease I, exonuclease VII, or SbcCD, are inviable without RecG. Removing RNase HI mimics the effect of removing RecG in that DrnhA cells are inviable if ExoI, ExoVII, and SbcCD are eliminated
-
physiological function
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mismatch repair proteins MutS and UvrD stimulate single-stranded DNA-specific exonuclease VII action on double-stranded DNA substrates. MutH and MutL proteins show no stimulation of exonuclease VII action. UvrD-mediated stimulation of exonuclease VII action on double-stranded DNA is not accompanied by strand separation. UvrD-mediated stimulation of exonuclease VII action on double-stranded DNA is accentuated by MutS and SSB proteins but not by MutL
physiological function
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to stay alive, cells must have either RecG or a 3'-single-stranded DNA exonuclease, which can be exonuclease I, exonuclease VII, or SbcCD. Cells lacking all three nucleases are inviable without RecG
physiological function
-
inactivation of exonuclease VII by a mutation in its large subunit xseA contributes to attenuation of DNA degradation in UV-irradiated recA mutants. The xseA mutation itself has only a weak effect, however, it acts synergistically with the xonA or sbcD mutations, which inactivate exonuclease I and SbcCD nuclease, respectively, in suppressing reckless DNA degradation. The quadruple xseA xonA sbcD recA mutants show no sign of DNA degradation during post-irradiation incubation, suggesting that ExoVII, together with ExoI and SbcCD, plays a crucial role in regulating RecBCD-catalyzed chromosome degradation. These nucleases may act on double-strand DNA breaks to create blunt DNA ends, the preferred substrates for the RecBCD enzyme. In UV-irradiated recF recA+ cells, the xseA, xonA, and sbcD mutations do not affect RecBCD-mediated DNA repair, suggesting that ExoVII, ExoI and SbcCD nucleases are not essential for the initial targeting of RecBCD to double-strand NA breaks
physiological function
exonuclease VII (ExoVII) of Escherichia coli is a single strand-specific DNA nuclease, exonuclease VII cleaves msDNA. The biochemical activity of XseA causing cell death is counteracted by the extra amount of the small subunit, XseB. Although the ability to induce cell death is not identical with the single-strand DNA specific nuclease activity, the residues important for nuclease activity are also important for lethality. The N-terminal domain of XseA causes cell death, and the chromosome is fragmented and condensed in the cells dying by XseA. Model for the function of XseA, overview
physiological function
the 3' exonucleases ExoI, ExoVII and SbcCD are involved in termination of DNA. Rinitiated at fork fusion intermediates can result in DNA replication which can sustain cell growth, overview. Levels of overreplication not correlate directly with the ability of cells to grow in the absence of origin firing
physiological function
-
to stay alive, cells must have either RecG or a 3'-single-stranded DNA exonuclease, which can be exonuclease I, exonuclease VII, or SbcCD. Cells lacking all three nucleases are inviable without RecG
-
additional information
under apoptotic conditions, the N-terminal domain of XseA is released from ExoVII through proteolysis by a caspase-like protease and the N-terminal fragment functions in the apoptosis-like cell death of Escherichia coli. ExoVII is composed of two different subunits encoded by xseA (large subunit) and xseB (small subunit) which are both required for catalytic activity
additional information
-
under apoptotic conditions, the N-terminal domain of XseA is released from ExoVII through proteolysis by a caspase-like protease and the N-terminal fragment functions in the apoptosis-like cell death of Escherichia coli. ExoVII is composed of two different subunits encoded by xseA (large subunit) and xseB (small subunit) which are both required for catalytic activity
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
-
heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
54000
-
heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
exonuclease VII of Escherichia coli is composed of two different subunits, the large subunit, XseA, and the small subunit, XseB
heterodimer
enzyme ExoVII consists of two subunits that are encoded by xseA and xseB. Gene xseA encodes the catalytically active subunit, while xseB encodes for a smaller subunit which is likely to regulate the activity of ExoVII
pentamer
additional information
-
stoichiometry of small to large subunits regulates ExoVII activity
pentamer
-
heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
pentamer
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heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structural analysis using bioinformatics. Large subunit XseA consists of four domains: an N-terminal OB-fold domain, a middle putatively catalytic domain, a coiled-coil domain and a short C-terminal segment. The OB-fold domain is responsible for DNA binding, the coiled-coil domain is involved in binding multiple copies of the XseB subunit and residues D155, R205, H238 and D241 of the middle domain are important for the catalytic activity but not for DNA binding
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A188T
site-directed mutagenesis of a highly conserved residue. The A188T mutant shows a msDNA cleavage indistinguishable from that of the wild-type, and lethality is reduced. About 10times more colonies are observed from the A188T mutant than from the wild-type
D155N
site-directed mutagenesis of a highly conserved residue. The D155N mutant loses the ability to cleave msDNA and displays little lethality
DELTA397-456
-
deletion mutant of large subunit XseA, complete loss of catalytic activity
G237R
site-directed mutagenesis of a residue in the glycine-rich motif. No msDNA cleavage is found for the G237R mutant but a low level of cell killing is still observed. The culture viability drops to about 30% after a 2 h induction
R64E/R68E/R69E
-
mutant of large subunit XseA, decrease in DNA-binding activity
additional information
additional information
-
construction of recD mutants showing a RecBC enzyme, instead of a RecBCD enzyme, lacking the RecD subunit and exonuclease VII activity, the mutation affects phage lambda red gam recombination, but does not cause an altered phenotype, overview
additional information
-
mutant in all four exonucleases (ExoI, ExoVII, ExoX, and RecJ) exhibits pronounced 20fold elevation of cross-overs between 25 bp of homology relative to the wild-type
additional information
-
recJ xseA sbcCD xonA2 quadruple mutants are cold sensitive depending on the xon allele. Absence of the two 3' exonucleases ExoI and ExoVII allows highly efficient conjugational recombination in recBCD+ cells, which is independent of SbcCD, recJ xseA double mutant has lower UV-survival than wild-type
additional information
-
conbstruction of ExoVII-deficient cells and of cells lacking alll three exonuxleases, exonuclease I, exonuclease VII, or SbcCD, phenotypes, detailed overview
additional information
-
construction of a series of subunit XseA deletion variants that lack one or several of the helices. Variants with a single helix deleted bind about 70% and variants with two helices deleted about 50% of the subunit XseB levels compared to the full-length XseA. All these deletion variants exhibit a complete loss of exonucleolytic activity in vitro
additional information
construction of ExoVII- (xseB) and ExoVII-(xseA) deficient mutant strains which are both inactive with msDNA. Construction of promoter deletion mutants, i.e. by deletion of entire promoter (large deletion from -125 to -11) or promoter-element mutation (-36T->C). Overexpression of the large subunit XseA is lethal, but the small subunit counteracts the toxicity of the large subunit. In samples containing both pCC-XseA and pT-XseB, overproduction of XseA by induction has little effect on the viability. RecA also protects cells from death by XseA overexpression. MsDNA cleavage and cell death at various subunit ratios, overview
additional information
-
construction of ExoVII- (xseB) and ExoVII-(xseA) deficient mutant strains which are both inactive with msDNA. Construction of promoter deletion mutants, i.e. by deletion of entire promoter (large deletion from -125 to -11) or promoter-element mutation (-36T->C). Overexpression of the large subunit XseA is lethal, but the small subunit counteracts the toxicity of the large subunit. In samples containing both pCC-XseA and pT-XseB, overproduction of XseA by induction has little effect on the viability. RecA also protects cells from death by XseA overexpression. MsDNA cleavage and cell death at various subunit ratios, overview
additional information
effect of xonA (ExoI), xseA (ExoVII) and sbcCD (SbcCD) mutations on growth without DnaA (dnaA46 at 42°C). The replication fork trap in the termination area is inactivated by deletion of tus and an rpoB*35 point mutation is introduced to alleviate replication-transcription conflicts resulting from replication forks travelling in a direction opposite to normal. The DnaA-independent growth is triggered by the absence of 3' exonucleases. Generation of RCe267 (dnaA46 DELTAtus rpo*), RCe528 (dnaA46 DELTAtus rpo* DELTAxonA), SLM1219 (dnaA46 DELTAtus rpo* DELTAxseA), RCe553 (dnaA46 DELTAtus rpo* DELTAsbcCD), SLM1194 (dnaA46 DELTAtus rpo* DELTAxonA* DELTAxseA), RCe554 (dnaA46 DELTAtus rpo* DELTAxonA DELTAsbcCD), SLM1223 (dnaA46 DELTAtus rpo* DELTAxseA DELTAsbcCD) and SLM1226 (dnaA46 DELTAtus rpo* DELTAxonA DELTAxseA DELTAsbcCD) mutant strains, phenotypes, overview. Overreplication of the termination area in cells lacking 3' exonucleases is abolished if the chromosome is linearized. And overreplication of the termination area in cells lacking 3' exonucleases requires PriA helicase activity. An asymmetric replichore arrangement does not increase overreplication of the termination area in cells lacking 3' exonucleases
additional information
-
effect of xonA (ExoI), xseA (ExoVII) and sbcCD (SbcCD) mutations on growth without DnaA (dnaA46 at 42°C). The replication fork trap in the termination area is inactivated by deletion of tus and an rpoB*35 point mutation is introduced to alleviate replication-transcription conflicts resulting from replication forks travelling in a direction opposite to normal. The DnaA-independent growth is triggered by the absence of 3' exonucleases. Generation of RCe267 (dnaA46 DELTAtus rpo*), RCe528 (dnaA46 DELTAtus rpo* DELTAxonA), SLM1219 (dnaA46 DELTAtus rpo* DELTAxseA), RCe553 (dnaA46 DELTAtus rpo* DELTAsbcCD), SLM1194 (dnaA46 DELTAtus rpo* DELTAxonA* DELTAxseA), RCe554 (dnaA46 DELTAtus rpo* DELTAxonA DELTAsbcCD), SLM1223 (dnaA46 DELTAtus rpo* DELTAxseA DELTAsbcCD) and SLM1226 (dnaA46 DELTAtus rpo* DELTAxonA DELTAxseA DELTAsbcCD) mutant strains, phenotypes, overview. Overreplication of the termination area in cells lacking 3' exonucleases is abolished if the chromosome is linearized. And overreplication of the termination area in cells lacking 3' exonucleases requires PriA helicase activity. An asymmetric replichore arrangement does not increase overreplication of the termination area in cells lacking 3' exonucleases
additional information
-
mutant in all four exonucleases (ExoI, ExoVII, ExoX, and RecJ) exhibits pronounced 20fold elevation of cross-overs between 25 bp of homology relative to the wild-type
-
additional information
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conbstruction of ExoVII-deficient cells and of cells lacking alll three exonuxleases, exonuclease I, exonuclease VII, or SbcCD, phenotypes, detailed overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris-HCl, pH 8, 10 mM mercaptoethanol, 0.1 mM EDTA, 0.2 M NaCl, 50% glycerol, 18 months, 10% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) purified by gel filtration and on nickel-NTA column
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wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) purified on nickel-NTA column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes xseA and xseB, overexpression of small subunit-encoding gene xseB in Escherichia coli, N- and C-terminal ends of large subunit-encoding xseA are separately amplified, cloned independently into a T-vector, and then joined together in pCC1fos, a vector with a very low copy number
strain deficient in enzymic activity plus deficiency in RecJ, ExoI and ExoX exonuclease activities as well as a strain deficient in RecJ, ExoVII and ExoI exonucleases grow poorly in presence of 2-aminopurine. Exposure to 2-aminopurine results in filament formation. The quadruple mutant is cold-sensitive with a severe growth defect at 30°C
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strain deficient in enzymic activity plus deficiency in RecJ, ExoI and ExoX exonuclease activities displays a 7fold increase in mutation rate, the availabilty of any one of thr nucleases is enough to support full mismatch correction
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wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) coexpressed in Escherichia coli BL21(DE3) cells
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