Any feedback?
Information on EC 3.1.11.5 - exodeoxyribonuclease V and Organism(s) Escherichia coli and UniProt Accession P07648
for references in articles please use BRENDA:EC3.1.11.5Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.11.5 exodeoxyribonuclease VSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
Synonyms
recbcd, recbcd enzyme, exonuclease v, escherichia coli recbcd, recbc dnase, recbcd exonuclease, addab enzyme, recbc nuclease, recbcd-type helicase-nuclease, exodeoxyribonuclease v, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E. coli ATP-dependent DNase
-
-
-
-
E. coli exonuclease V
-
-
-
-
Escherichia coli exonuclease V
-
-
-
-
Escherichia coli RecBCD
-
-
-
-
Exodeoxyribonuclease V 125 kDa polypeptide
-
-
-
-
Exodeoxyribonuclease V 135 KDA polypeptide
-
-
-
-
Exodeoxyribonuclease V 67 kDa polypeptide
-
-
-
-
exonuclease V
gene recBC DNase
-
-
-
-
gene RecBC endoenzyme
-
-
-
-
nuclease, exodeoxyribo V
-
-
-
-
recBC deoxyribonuclease
-
-
-
-
recBC DNase
-
-
-
-
recBC nuclease
-
-
-
-
RecBCD
recBCD enzyme
exonuclease V
-
-
-
-
recBCD enzyme
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
preference for double-stranded DNA, possesses DNA-dependent ATPase activity, acts endonucleolytically on single-stranded circular DNA
-
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
mechanism, The enzyme is an ATP-dependent DNA exonuclease and a helicase, its exonuclease activity is subject to regulation by an octameric nucleotide sequence called chi.
-
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
The enzyme generates 3 single-stranded DNA ends used by RecA for homologous recombination. The exonuclease activity is altered when the enzyme encounters a Chi sequence, 5-GCTGGTGG-3, in double-stranded DNA, an event critical to generation of 3 single-stranded DNA. Chi recognition requires that Chi be flanked by DNA at either end. A specific site for Chi recognition exists on enzyme, which binds Chi with greater affinity than a non-Chi sequence and is probably adjacent to non-specific DNA binding sites.
-
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
The enzyme is involved initiating DNA recombination. The nuclease properties of the enzyme are regulated upon recognition of a specific DNA sequence by the translocating enzyme. This sequence, called chi, corresponds to the octamer 5-GCTGGTGG-3.
-
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
The enzyme is required for homologous recombination and DNA repair, the degradative and recombinational activities of enzyme, as well as its structure, are regulated by a specific DNA sequence called Chi. The recombination requires loading of RecA by RecBCD enzyme and that the RecD subunit inhibits this reaction.
-
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides
the enzyme complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DNA-dependent ATPase activity
-
-
-
-
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37350-26-8
-
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
34-mer ssDNA + H2O
?
-
REcB30 binds more tightly on ssDNA than on dsDNA but is more active on dsDNA than on ssDNA
-
-
?
double-stranded DNA
3'-ended stretch of single-stranded DNA
-
the enzyme is a ATP dependent helicase and exonuclease
-
?
double-stranded DNA
single stranged DNA
-
unwinding of double-stranded DNA
substrate for the DNA strand-exchange protein, RecA, model for chi-induced RecA protein loading by RecBCD enzyme, substrate for the DNA strand-exchange protein, RecA
?
double-stranded DNA
single-stranded DNA
-
ATP-dependent, unwinding of DNA molecule
-
?
dsDNA + H2O
?
-
REcB30 binds more tightly on ssDNA than on dsDNA but is more active on dsDNA than on ssDNA
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
individual RecB protein has ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
RNA-DNA hybrids or cross-linked DNA can serve as cofactors
-
-
?
ATP + H2O
ADP + phosphate
-
complete inhibition of DNAse activity has no effect on ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
biphasic activity represents DNA unwinding and ATPase activity
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
-
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
mechanism
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
unwinding in the presence of E. coli binding protein SSB or high levels of ATP
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
no recombination in recB2109CD mutants and abc-modified recBCD mutants
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
reduced unwinding activity in abc-modified recBCD protein
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
loop is formed on the same strand that is cut by the enzyme near chi
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
unwinding activity in the recBC enzyme
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
no unwinding on replicative form DNA
-
-
?
double-stranded DNA
intermediates with single stranded regions
-
recB2109CD mutant has no chi nicking activity
-
-
?
double-stranded DNA
single-stranded DNA fragments
-
ATP dependent double-stranded DNA exonuclease and processive DNA helicase
-
?
double-stranded DNA
single-stranded DNA fragments
-
the enzyme plays a an important role in the initiation of DNA recombination and recombinant-dependent DNA replication
-
?
double-stranded DNA + H2O
?
-
BL21 and BL21-RecD-SBP strains share similar linear DNA degradation activities
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
-
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
no exonuclease activity in recD null mutants
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
slower degradation of UV-irradiated DNA
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
reduced activity in abc-modified recBCD protein
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
supplies nucleotides for break repair of DNA
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
acts on native, heat-denatured and glucosylated DNA
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
reduced activity in recB2109CD mutant
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
a gap of 5 nucleotides in circular DNA needed for activity
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
no activity on circular DNA
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
can release pyrimidine primer from UV-irradiated DNA
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
only ATP-dependent exonuclease activity is altered in thermolabile recB and recC mutants
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
ATP dependent double-stranded DNA exonuclease
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
responsible for several steps in genetic recombination process
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
ATP-dependent exonuclease
133994, 133995, 133996, 133997, 133998, 133999, 134000, 134001, 134002, 134003, 134004, 134012, 134013, 134023, 134025, 134026, 134027, 134028, 134029, 134030, 134031
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
ATP-dependent helicase
-
-
?
douple-stranded DNA
?
-
the enzyme has potent nuclease and helicase activity
-
?
douple-stranded DNA
?
-
the enzyme is required for the major pathway of double-strand DNA break repair and genetic exchange, the enzyme has potent nuclease and helicase activity
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
-
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
no exonuclease activity in recD null mutants
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
reduced activity in recB2109CD mutant
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
endonuclease activity is ATP dependent in recBC enzyme
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
also endonuclease activity on circular DNA
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP dependence varies
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
rate of degradation is less than double-stranded DNA
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
no stimulation with ATP
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-dependent exonuclease
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-dependent endonuclease
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-stimulated endonuclease
-
-
?
additional information
?
-
the RecA protein loading is an essential function of the enzyme
-
?
additional information
?
-
-
first: The enzyme is a potent double-stranded DNA exonuclease that destroys linear DNA produced by restriction of foreign DNA. second: The enzyme promotes repair of double-stranded DNA breaks and genetic recombination in the vicinity of chi recombination hotspots.
-
?
additional information
?
-
-
the activities of enzyme responsible for the initiation of recombinantional and repair processes are required for UV-induced restriction alleviation
-
?
additional information
?
-
-
The enzyme is involved in the radiation-induced process know as prophage inactivation. The helicase activity of enzyme is responsible for the progressive loss of prophage recombinogenicity. This loss is most probably a consequence of the unsuccessful enzyme-dependent recombinational repair of double-stranded breaks in the cell chromosome, during which some structures unsuitable for further recombination reactions may be produced.
-
?
additional information
?
-
-
nucleolytic degradation of DNA by RecBCD is not necessary for intracellular Chi hotspot activity. Nicking of DNA by RecBCD enzyme at Chi is sufficient
-
-
?
additional information
?
-
-
RecBCD enzyme is a multifunctional heterotrimeric complex that possesses processive helicase and exonuclease activities. Upon encountering the DNA regulatory sequence, chi, the enzymatic properties of RecBCD enzyme are altered. Its helicase activity is reduced, the 3'-5' nuclease activity is attenuated, the 5'-3' nuclease activity is up-regulated, and it manifests an ability to load RecA protein onto single-stranded DNA. The net result of these changes is the production of a highly recombinogenic structure known as the presynaptic filament
-
-
?
additional information
?
-
-
RecD subunit signals the RecB subunit to cut DNA. the existence of a cascade of intersubunit signals from Chi-RecC to RecD to RecB is proposed
-
-
?
additional information
?
-
-
the nuclease reactions of the RecBCD-DNA complexes are initiated by mixing with ATP. The reaction is processive. The reaction begins near the 3'-end of the [5'-32P]DNA substrates and the major cleavage sites are two to four phosphodiester bonds apart. DNA cleavage is tightly coordinated with movement of the enzyme along the DNA. The reaction time-courses at low concentrations of ATP (0.1 mM and 0.025 mM) have a significant lag before cleavage products appear. We propose that the lag represents ATP-dependent movement of the DNA from an initial binding site in the helicase domain of the RecB subunit to the nuclease active site in a separate domain of RecB
-
-
?
additional information
?
-
the RecB nuclease domain affects the interaction of RecBC with the end of the 3'-ssDNA tail
-
-
?
additional information
?
-
-
the RecB nuclease domain affects the interaction of RecBC with the end of the 3'-ssDNA tail
-
-
?
additional information
?
-
-
RecD protein expression level is decreased at lower cultivation temperature, which greatly improves the productivity of cell-free protein synthesis from linear DNA templates
-
-
?
additional information
?
-
RecBCD degradation of DNA is inhibited by either cisplatin-damaged or UV-damaged DNA sequences
-
-
?
additional information
?
-
assay substrate is PvuII-cut plasmid DNA. when the RecBCD enzyme encounters a Chi site (5'-GCTGGTGG), translocation of the RecBCD pauses and the nuclease digestion of the 30-tail stops
-
-
?
additional information
?
-
when the concentration of ATP is greater than that of Mg2+ ions, RecBCD unwinds the DNA and nicks the Chi-containing strand of DNA a few nucleotides to the 3' side of the core sequence, continued unwinding produces 3'-ended ssDNA for strand exchange by RecA. When the concentration of Mg2+ ions is greater than that of ATP, RecBCD makes, during unwinding, occasional endonucleolytic nicks up to Chi on the 3'-ended strand, releasing fragments hundreds of nucleotides long, continued unwinding and similar nicking of the complementary strand produces 3'-ended ssDNA for strand exchange. A second round of RecBCD action is required to produce the acid-soluble, short oligonucleotides typically assayed as nuclease activity with purified enzyme and in repair-deficient cells (e.g. recA mutants) after DNA damage
-
-
?
additional information
?
-
-
when the concentration of ATP is greater than that of Mg2+ ions, RecBCD unwinds the DNA and nicks the Chi-containing strand of DNA a few nucleotides to the 3' side of the core sequence, continued unwinding produces 3'-ended ssDNA for strand exchange by RecA. When the concentration of Mg2+ ions is greater than that of ATP, RecBCD makes, during unwinding, occasional endonucleolytic nicks up to Chi on the 3'-ended strand, releasing fragments hundreds of nucleotides long, continued unwinding and similar nicking of the complementary strand produces 3'-ended ssDNA for strand exchange. A second round of RecBCD action is required to produce the acid-soluble, short oligonucleotides typically assayed as nuclease activity with purified enzyme and in repair-deficient cells (e.g. recA mutants) after DNA damage
-
-
?
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
double-stranded DNA
single stranged DNA
-
unwinding of double-stranded DNA
substrate for the DNA strand-exchange protein, RecA
?
double-stranded DNA
single-stranded DNA
-
ATP-dependent, unwinding of DNA molecule
-
?
double-stranded DNA
single-stranded DNA fragments
-
the enzyme plays a an important role in the initiation of DNA recombination and recombinant-dependent DNA replication
-
?
douple-stranded DNA
?
-
the enzyme is required for the major pathway of double-strand DNA break repair and genetic exchange, the enzyme has potent nuclease and helicase activity
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
responsible for several steps in genetic recombination process
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
ATP-dependent exonuclease
133994, 133995, 133996, 133997, 133998, 133999, 134000, 134001, 134002, 134003, 134004, 134012, 134013, 134023, 134025, 134026, 134027, 134028, 134029, 134030, 134031
-
-
?
double-stranded DNA + H2O
single-stranded DNA fragments
-
ATP-dependent helicase
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
-
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-dependent exonuclease
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-dependent endonuclease
-
-
?
single stranded DNA + H2O
5'-phosphomonoester oligonucleotides
-
ATP-stimulated endonuclease
-
-
?
additional information
?
-
the RecA protein loading is an essential function of the enzyme
-
?
additional information
?
-
-
first: The enzyme is a potent double-stranded DNA exonuclease that destroys linear DNA produced by restriction of foreign DNA. second: The enzyme promotes repair of double-stranded DNA breaks and genetic recombination in the vicinity of chi recombination hotspots.
-
?
additional information
?
-
-
the activities of enzyme responsible for the initiation of recombinantional and repair processes are required for UV-induced restriction alleviation
-
?
additional information
?
-
-
The enzyme is involved in the radiation-induced process know as prophage inactivation. The helicase activity of enzyme is responsible for the progressive loss of prophage recombinogenicity. This loss is most probably a consequence of the unsuccessful enzyme-dependent recombinational repair of double-stranded breaks in the cell chromosome, during which some structures unsuitable for further recombination reactions may be produced.
-
?
additional information
?
-
-
RecD protein expression level is decreased at lower cultivation temperature, which greatly improves the productivity of cell-free protein synthesis from linear DNA templates
-
-
?
additional information
?
-
RecBCD degradation of DNA is inhibited by either cisplatin-damaged or UV-damaged DNA sequences
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the ATP analogue ADPNP binds in the ATP-binding site of the RecB subunit
-
ATP
when the concentration of ATP is greater than that of Mg2+ ions, RecBCD unwinds the DNA and nicks the Chi-containing strand of DNA a few nucleotides to the 3' side of the core sequence, continued unwinding produces 3'-ended ss DNA for strand exchange by RecA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Ca2+
-
double-stranded DNA exonuclease and single-stranded DNA exonuclease and endonuclease activities completely inhibited
Mg2+
the nuclease activities of wild-type enzyme is sensitive to the concentration of free magnesium ions in solution
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abc protein
-
anti recBCD; binds the recBCD enzyme and inhibits recombination but not exonuclease activity; gamma-protein analog encoded by bacteriophage P22
-
bacteriophage Mu
-
induction of bacteriophage Mu causes inhibition of exonuclease V
-
ATP
-
0.2 mM and higher concentrations inhibits phosphodiester hydrolysis; neither the rate nor the extent of hydrolysis of single-stranded DNA nor ATP is affected
E. coli single stranded DNA binding protein
-
ATPase activity complete inhibited by SSB
-
Gamma-protein
-
binds the recBCD enzyme and inhibits ATPase, exonuclease and endonuclease and helicase activity
-
additional information
-
The overall inhibition is length dependent, the longer the oligonucleotide the more effective the inhibition. The oligonucleotide Chi+ oligonucletides inhibit the activities of enzyme much more than do the oligonucleotides Chi0.
-
additional information
-
lambda Gam, by inhibiting host RecBCD nuclease activity, helps to improve the efficiency of lambda Red-mediated recombination with linear double-strand DNA
-
additional information
RecBCD degradation of DNA is inhibited by either cisplatin-damaged or UV-damaged DNA sequences. A DNA-targeted 9-aminoacridinecarboxamide cisplatin analogue is also found to inhibit RecBCD activity. The three different DNA damaging agents, UV light, cisplatin and 9AmAcPtCl2, are examined, all strongly inhibit the activity of RecBCD
-
additional information
the tether (amino acids 881-899 of RecB) amino-acid composition, like the tether length, can strongly affect the ability ofRecBCD to respond to Chi and to promote recombination
-
additional information
-
the tether (amino acids 881-899 of RecB) amino-acid composition, like the tether length, can strongly affect the ability ofRecBCD to respond to Chi and to promote recombination
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
mechanism of nuclease activation, an alpha-helix (residues 913-922) within the linker region (residues 870-940) of RecB, that connects the C-terminal nuclease domain to the N-terminal helicase domains, sits in the nuclease active site thus blocking access, overview. The nuclease activity of the RecBCD complex is attenuated in the initiation complex prior to binding ATP, because the nuclease requires ssDNA to be fed into it by the helicase activities of the complex
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
The corrected unwinding rate is 443 base pairs 1/sec, which is due to a single molecule of enzyme that bound to the free double-stranded DNA end opposite the bead, and both translocates and unwinds the DNA in an ATP-dependent manner once the DNA entered the ATP channel. The rate of unwinding increases with increasing ATP concentration and increasing temperature
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 37
-
The rate of unwinding in 1 mM ATP increases twofold when the temperature is raised from 23°C to 37°C.
25 - 37
additional information
-
by altering the cultivation temperature (37°C) of the cells to a moderately lower range (20-34°C), dramatically reduces the linear DNA degradation activity of RecD
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
133946, 133978, 133996, 133997, 133999, 134001, 134003, 134004, 134005, 134006, 134007, 134008, 134009, 134010, 134011, 134012, 134013, 134015, 134023, 134024, 134026, 134027, 134028, 134029, 134031, 134034, 651426, 652076, 652814, 653270, 653336, 653394, 653653, 653863, 664124, 666437, 678488, 680012, 680025, 681389, 681405, 682582, 716395, 730828
-
-
RecB beta chain and REcD alpha chain and Rec C gamma chain
UniProt
RecBCD enzyme subunits RecB, RecC, and RecD, i.e. beta-, gamma-, and alpha-subunits
UniProt
thermosensitive mutants with thermolabile adenosine 5'-triphosphate-dependent exonucleolytic hydrolysis of duplex DNA
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
enzyme RecBCD's repair of DNA is controlled by Chi, overview
metabolism
the RecBCD/AddAB complexes are highly processive helicase/nuclease machines that digest DNA from the broken end until they encounter a crossover hotspot instigator (Chi) sequence. At this point their activities are modulated to produce a 3-tailed duplex onto which RecA is loaded
physiological function
-
type I DNA restriction/modification systems are oligomeric enzymes capable of switching between a methyltransferase function on hemimethylated host DNA and an endonuclease function on unmethylated foreign DNA. Reuse of the methyltransferase subunits is possible so that restriction proceeds until the restriction subunits are depleted. RecBCD exonuclease halts restriction and does not assist recycling, influence of RecBCD on the EcoKI type I restriction enzyme, overview
physiological function
-
after transposition of phage Mu into the Escherichia coli chromosome, the flanking DNA is degraded, and the 5-bp gaps left in the target are repaired to generate a simple Mu insertion. The first event in repair is removal of the flanking DNA by RecBCD exonuclease, whose entry past the N-protein block is licensed by the transpososome. When RecBCD is allowed entry into the flanking DNA, it degrades this DNA until it arrives at the transpososome, which presents a barrier for further RecBCD movement. RecBCD action is required for stimulating endonucleolytic cleavage within the transpososome-protected DNA, leaving 4-nt flanks outside both Mu ends
physiological function
RecBCD (exonuclease V) plays a critical role in recombinational DNA repair. Escherichia coli RecBCD is involved in recombinational repair of double-strand breaks that are caused by defective DNA replication and other DNA damaging agents. Unrepaired DNA damage caused by cisplatin or UV light can lead to defective DNA replication and the production of double-strand breaks. Presence of adducts on the DNA double-helix can have major consequences for the efficient functioning of DNA repair enzymes. Escherichia coli RecBCD (exonuclease V) is involved in recombinational repair of double-strand breaks that are caused by defective DNA replication, DNA damaging agents and other factors. The holoenzyme possesses a bipolar helicase activity which helps unwind DNA from both 3'- and 5'-directions and is coupled with a potent exonuclease activity that is also capable of digesting DNA from both 3'- and 5'-ends
physiological function
RecBCD-type helicase-nuclease (RecBCD) catalyses the processing of double-stranded DNA breaks for repair by homologous recombination. The enzyme complex is a highly processive, duplex unwinding and degrading machine that requires tight regulation. The nuclease activity of the complex is activated once unwinding progresses
physiological function
repair of DNA double-strand breaks uses a highly conserved helicase-nuclease complex to unwind DNA from a broken end and cut it at specific DNA sequences called Chi. In Escherichia coli the RecBCD enzyme also loads the DNA strand exchange protein RecA onto the newly formed end, resulting in a recombination hotspot at Chi. Chi hotspots regulate multiple RecBCD activities by altering RecBCD's conformation, which is proposed to include the swinging of the RecB nuclease domain on the 19-amino-acid tether connecting the helicase and nuclease domains. Proper control of RecBCD by Chi requires that the tether be long enough and appropriately flexible. A model, in which the swing-time of the nuclease domain determines the position of Chi-dependent and Chi-independent cuts and Chi hotspot activity, is established. Generation of a molecular model for Chi-dependent nuclease swinging, and predictions of the nuclease-swing model, overview
additional information
the SH3 domain interacts with the ssDNA tail in a location different to that normally occupied by a peptide in canonical eukaryotic SH3 domains, thus retaining the potential to bind peptide at the same time as the ssDNA tail, interactions with the 5'-tail and the RecD subunit, overview. The N-terminal domain of RecD contacts the 2B domain of RecC and the conformational change in RecD has significant effects on the conformation of the RecC subunit. The RecB nuclease domain bridges a gap between the 1A and 2B domains of RecC and the conformational changes cause a significant shift in position of the RecB nuclease relative to these domains that reveals the mechanism for nuclease activation. Interaction between the 2B domain of RecD and the RecB subunit has a number of consequences, analysis of conformational changes that proceed from the initiation complex to nuclease activation
additional information
the tether (amino acids 881-899) of RecB is essential for Chi's stimulation of recombination. The tether can be lengthened somewhat without alteration of Chi's control, but a too-long tether significantly reduces Chi's control of RecBCD
additional information
-
the tether (amino acids 881-899) of RecB is essential for Chi's stimulation of recombination. The tether can be lengthened somewhat without alteration of Chi's control, but a too-long tether significantly reduces Chi's control of RecBCD
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
270000
350000
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
trimer
additional information
structure of the SH3-fold RecD 2B domain, overview
heterotrimer
-
RecB, RecC and RecD subunits, The nuclease active site on the RecB 30000 Da domain is the universal nuclease active site of enzyme that is responsible for single-stranded DNA degradation in both directions.
heterotrimer
-
RecB, RecC and RecD, The C-terminus of RecC: 35000 Da, is required for assembly of the RecD subunit into enzyme holoenzyme but not for recombination proficiency. The N-terminus of RecC: 95000 Da, contains functions essential for recombination and is also required for chi activity. RecD is essential for nuclease activity, regulation by the recombination hotspot Chi, and high affinity for DNA ends. RecC interacts with RecD to form a heterotrimer only in the presence of RecB.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complex RecBCD bound with a DNA substrate (a 350 kDa complex) or ATP analogue ADPNP, mixing of 0.0015 ml of 5 mg/ml protein, and a 1.75fold excess of DNA, 2 mM ADPNP, and 4 mM MgCl2, in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM TCEP, with 0.03 ml of 0.1% detergent n-dodecyl beta-D-maltoside on ice, incubation at 4°C overnight, X-ray diffraction structure determination and analysis at 3.8 A resolution, molecular replacement and modelling using the crystal structure of RecBCD in complex with an extended DNA fork (PDB ID 3K70) as a template
vapour-diffusion hanging drop method, crystal structure of a complex of Escherichia coli RecBCD enzyme bound to ablunt-ended DNA hairpin
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D1067A
D1080A
K1082A
-
chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
K1082Q
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit abolishes nuclease activity on both single- and double-stranded DNA but the mutant enzyme is active as helicase. The mutant is unable to produce chi-specific fragments from either strand of a chi-containing double-stranded DNA substrate.
Y1081A
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity.
Y1081F
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity.
Y1114A
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity.
Y1114F
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity.
additional information
D1067A
-
chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
D1067A
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit abolishes nuclease activity on both single- and double-stranded DNA but the mutant enzyme is active as helicase. The mutant is unable to produce chi-specific fragments from either strand of a chi-containing double-stranded DNA substrate.
D1080A
-
chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
D1080A
-
Comparison: recB(D1080A)CD is recombinant-deficient, and sensitive to DNA damaging agents, and the purified enzyme failed to load RecA during DNA winding. recB(D1080A)C is recombinant-proficient and resistant to DNA damaging agents, and the mutant is active RecA loading assay.
additional information
-
in mutants carrying either recB2109 or recD1903, which do not exhibit significant nuclease activities, the prophage progressively loses its capacity for both site-specific and general recombination
additional information
-
RecB mutants that cannot bind or hydrolyze ATP are completely defective for DNA recombination
additional information
-
recBC1010D, recBC1041D and recBCD1013 mutants have less than 0.2% of the exonuclease activity of wild-type enzyme. recBC1010D and recBC1041D produce RecD but fail to assemble it into holoenzyme
additional information
the mutant RecB2109CD degrades the double-stranded DNA primarily in the 5 to 3 direction, producing processed double-stranded DNA with a 3-terminal overhang, the mutant is unable to coordinate the loading of RecA protein onto the single-stranded DNA produced, this inability can be responsible for recB2109 recombination defect observed in vivo
additional information
-
the recombination deficiency of the RecBC1004D-chi interaction can be overcome by the enhanced ability of RecA730 to assemble on single-stranded DNA in vitro and in vivo
additional information
deletion of amino acids 881-899 (DELTA19) of RecB, the entire tether. The resulting mutant DELTA19 is recombination-deficient and has no detectable Chi activity. The mutant retained nuclease activity, demonstrating that it is not a null mutant. Additional construction of RecB mutants lacking one or another part of the tether. Inserting two foreign tethers, to make the tether 57 amino acids long, both reduce Chi activity and recombination proficiency to about the same level as that of RecBCD with the 38-amino-acid tethers. None of the mutants reported increases Chi hotspot activity. RecBCD enzymatic activities coincide with the genetic activities of the tether mutants
additional information
-
deletion of amino acids 881-899 (DELTA19) of RecB, the entire tether. The resulting mutant DELTA19 is recombination-deficient and has no detectable Chi activity. The mutant retained nuclease activity, demonstrating that it is not a null mutant. Additional construction of RecB mutants lacking one or another part of the tether. Inserting two foreign tethers, to make the tether 57 amino acids long, both reduce Chi activity and recombination proficiency to about the same level as that of RecBCD with the 38-amino-acid tethers. None of the mutants reported increases Chi hotspot activity. RecBCD enzymatic activities coincide with the genetic activities of the tether mutants
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant D1080A enzyme complexes from Escherichia coli by nickel affinity chromatography, heparin affinity chromatography, dialysis, and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes recBCD, recombinant expression in Escherichia coli strain V2831
genes recBCD, recombinant expression of His-tagged wild-type and mutant D1080A enzyme complexes from three plasmids, pETduet-His6-TEVsite-recBD1080A, pRSFduet-recC and pCDFduet-recD in a DrecBD in Escherichia coli
RecD overproduction prevents dissociation of RscBCD enzyme from DNA substrate and increases its processivity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
cloning of palyndromic structures in the Physarum actin gene in E. coli lacking the recBC gene
analysis
-
lack of enzyme increases transfection frequencies with linear DNA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bassett, C.L.; Kushner, S.R.
Exonucleases I, III, and V are required for stability of ColE1-related plasmids in Escherichia coli
J. Bacteriol.
157
661-664
1984
Escherichia coli
Lehman, I.R.
Bacterial deoxyribonucleases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
251-270
1971
Escherichia coli
-
Hoekstra, W.P.; Bergmans, J.E.; Zuidweg, E.M.
Role of recBC nuclease in Escherichia coli transformation
J. Bacteriol.
143
1031-1032
1980
Escherichia coli
Telander Muskavitch, K.M.; Linn, S.
recBC-like enzymes:exonuclease V deoxyribonucleases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
14
233-250
1981
Alcaligenes faecalis, Bacillus cereus, Bacillus subtilis, Brevibacillus laterosporus, Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Micrococcus luteus, Mycolicibacterium smegmatis, Pseudomonas aeruginosa, Strongylocentrotus intermedius
-
Goldmark, P.J.; Linn, S.
Purification and properties of the recBC DNase of Escherichia coli K-12
J. Biol. Chem.
247
1849-1860
1972
Escherichia coli
Wright, M.; Buttin, G.
The isolation and characterization from Escherichia coli of an adenosine triphosphate-dependent deoxyribonuclease directed by rec B, C genes
J. Biol. Chem.
246
6543-6555
1971
Escherichia coli
Oishi, M.
An ATP-dependent deoxyribonuclease from Escherichia coli with a possible role in genetic recombination
Proc. Natl. Acad. Sci. USA
64
1292-1299
1969
Escherichia coli
Karu, A.E.; MacKay, V.; Goldmark, P.J.; Linn, S.
The recBC deoxyribonuclease of Escherichia coli K-12. Substrate specificity and reaction intermediates
J. Biol. Chem.
248
4874-4884
1973
Escherichia coli
Kushner, S.R.
Differential thermolability of exonuclease and endonuclease activities of the recBC nuclease isolated from thermosensitive recB and recC mutants
J. Bacteriol.
120
1219-1222
1974
Escherichia coli
Tanaka, J.; Sekiguchi, M.
Action of exonuclease V (the recBC enzyme) on ultraviolet-irradiated DNA
Biochim. Biophys. Acta
383
178-187
1975
Escherichia coli
Van Dorp, B.; Benne, R.; Palitti, F.
The ATP-dependent DNAase from Escherichia coli rorA: a nuclease with changed enzymatic properties
Biochim. Biophys. Acta
395
446-454
1975
Escherichia coli
Karu, A.E.; Sakaki, Y.; Echols, H.; Linn, S.
The gamma protein specified by bacteriophage gamma. Structure and inhibitory activity for the recBC enzyme of Escherichia coli
J. Biol. Chem.
250
7377-7387
1975
Escherichia coli
Eichler, D.C.; Lehman, I.R.
On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli
J. Biol. Chem.
252
499-503
1977
Escherichia coli
Rosamond, J.; Telander, K.M.; Linn S.
Modulation of the action of the recBC enzyme of Escherichia coli K-12 by Ca2+
J. Biol. Chem.
254
8646-8652
1979
Escherichia coli
Dykstra, C.C.; Prasher, D.; Kushner, S.R.
Physical and biochemical analysis of the cloned recB and recC genes of Escherichia coli K-12
J. Bacteriol.
157
21-27
1984
Escherichia coli
Finch, P.W.; Storey, A.; Brown, K.; Brown, K.; Hickson, I.D.; Emmerson, P.T.
Complete nucleotide sequence of recD, the structural gene for the alpha subunit of Exonuclease V of Escherichia coli
Nucleic Acids Res.
14
8583-8594
1986
Escherichia coli
Finch, P.W.; Storey, A.; Chapman, K.E.; Hickson, I.D.; Emmerson, P.T.
Complete nucleotide sequence of the Escherichia coli recB gene
Nucleic Acids Res.
14
8573-8582
1986
Escherichia coli
Braedt, G.; Smith, G.R.
Strand specificity of DNA unwinding by RecBCD enzyme
Proc. Natl. Acad. Sci. USA
86
871-875
1989
Escherichia coli
Roman, L.J.; Kowalczykowski, S.C.
Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: relationship of ATP hydrolysis to the unwinding of duplex DNA
Biochemistry
28
2873-2881
1989
Escherichia coli
Roman, L.J.; Kowalczykowski, S.C.
Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
Biochemistry
28
2863-2873
1989
Escherichia coli
Telander Muskavitch, K.M.; Linn, S.
A unified mechanism for the nuclease and unwinding activities of the recBC enzyme of Escherichia coli
J. Biol. Chem.
257
2641-2648
1982
Escherichia coli
Schaus, N.A.; Wright, A.
Inhibition of Escherichia coli exonuclease V by bacteriophage Mu
Virology
102
214-217
1980
Escherichia coli
Dykstra, C.C.; Palas, K.M.; Kushner, S.R.
Purification and characterization of exonuclease V from Escherichia coli K-12
Cold Spring Harbor Symp. Quant. Biol.
49
463-467
1989
Escherichia coli
-
Banfalvi, G.; Csuzi, S.; Antoni, F.
Resolution and reconstitution of the rec BC deoxyribonuclease of Escherichia coli
FEBS Lett.
164
28-32
1983
Escherichia coli
Nader, W.F.; Edlind, T.D.; Huettermann, A.; Sauer, H.W.
Cloning of Physarum actin sequences in an exonuclease-deficient bacterial host
Proc. Natl. Acad. Sci. USA
82
2698-2702
1985
Escherichia coli
Amundsen, S.K.; Taylor, A.F.; Chaudhury, A.M.; Smith, G.R.
recD: the gene for an essential third subunit of exonuclease V
Proc. Natl. Acad. Sci. USA
83
5558-5562
1986
Escherichia coli
Palas, K.M.; Kushner, S.R.
Biochemical and physical characterization of exonuclease V from Escherichia coli. Comparison of the catalytic activities of the RecBC and RecBCD enzymes
J. Biol. Chem.
265
3447-3454
1990
Escherichia coli
Murphy, K.C.
Lambda Gam protein inhibits the helicase and chi-stimulated recombination activities of Escherichia coli RecBCD enzyme
J. Bacteriol.
173
5808-5821
1991
Escherichia coli
Boehmer, P.E.; Emmerson, P.T.
Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits
Gene
102
1-6
1991
Escherichia coli
Masterson, C.; Boehmer, P.E.; McDonald, F.; Chaudhuri, S.; Hickson, I.D.; Emmerson, P.T.
Reconstitution of the activities of the RecBCD holoenzyme of Escherichia coli from the purified subunits
J. Biol. Chem.
267
13564-13572
1992
Escherichia coli
Eggleston, A.K.; Kowalczykowski, S.C.
Biochemical characterization of a mutant recBCD enzyme, the recB2109CD enzyme, which lacks chi-specific, but not non-specific, nuclease activity
J. Mol. Biol.
231
605-620
1993
Escherichia coli
Murphy, K.C.
Biochemical characterization of P22 phage-modified Escherichia coli RecBCD enzyme
J. Biol. Chem.
269
22507-22516
1994
Escherichia coli
Waldstein, E.A.
Role of exonuclease V and VIII in adenosine 5'-triphosphate- and deoxynucleotide triphosphate-dependent strand break repair in toluenized Escherichia coli cells treated with X rays
J. Bacteriol.
139
1-7
1979
Escherichia coli
Amundsen, S.K.; Taylor, A.F.; Smith, G.R.
A domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme
Genetics
161
483-492
2002
Escherichia coli
Arnold, D.A.; Kowalczykowski, S.C.
Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme
J. Biol. Chem.
275
12261-12265
2000
Escherichia coli (P08394)
Wang, J.; Chen, R.; Julin, D.A.
A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions
J. Biol. Chem.
275
507-513
2000
Escherichia coli
Churchill, J.J.; Kowalczykowski, S.C.
Identification of the RecA Protein-loading Domain of RecBCD Enzyme
J. Mol. Biol.
297
537-542
2000
Escherichia coli
Jockovich, M.E.; Myers, R.S.
Nuclease activity is essential for RecBCD recombination in Escherichia coli
Mol. Microbiol.
41
949-962
2001
Escherichia coli
Chedin, F.; Kowalczykowski, S.C.
A novel family of regulated helicases/nucleases from Gram-positive bacteria: insights into the initiation of DNA recombination
Mol. Microbiol.
43
823-834
2002
Bacillus subtilis, Escherichia coli
Blanco, P.R.; Brewer, L.R.; Corzett, M.; Balhorn, R.; Yeh, Y.; Kowalczykowski, S.C.; Baskin, R.J.
Processive translocation and DNA unwinding by individual RecBCD enzyme molecules
Nature
409
374-378
2001
Escherichia coli
Kulkarni, A.; Julin, D.A.
Specific inhibition of the E.coli RecBCD enzyme by Chi sequences in single-stranded oligodeoxyribonucleotides
Nucleic Acids Res.
32
3672-3682
2004
Escherichia coli
Cajo, G.C.; Brcic-Kostic, K.; Ivancic, I.; Trgovcevic, Z.; Salaj-Smic, E.
Inactivation of the EcoKI restriction in UV-irradiated Escherichia coli: The role of RecBCD enzyme
Periodicum Biologorum
103
157-161
2001
Escherichia coli
-
Amundsen, S.K.; Taylor, A.F.; Smith, G.R.
The RecD subunit of the Escherichia coli RecBCD enzyme inhibits RecA loading, homologous recombination, and DNA repair
Proc. Natl. Acad. Sci. USA
97
7399-7404
2000
Escherichia coli
Vlahovic, K.; Petranovic, M.; Zahradka, D.; Petranovic, D.
Progressive loss of lambda prophage recombinogenicity in UV-irradiated Escherichia coli: the role of RecBCD enzyme
Res. Microbiol.
151
727-738
2000
Escherichia coli
Sun, J.Z.; Julin, D.A.; Hu, J.S.
The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA
Biochemistry
45
131-140
2006
Escherichia coli
Singleton, M.R.; Dillingham, M.S.; Gaudier, M.; Kowalczykowski, S.C.; Wigley, D.B.
Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks
Nature
432
187-193
2004
Escherichia coli
Dermic, D.; Dermic, E.; Zahradka, D.; Petranovic, M.; Lers, N.
gamma-Irradiated RecD overproducers become permanent recB-/C- phenocopies for extrachromosomal DNA processing due to prolonged titration of RecBCD enzyme on damaged Escherichia coli chromosome
Biochimie
88
379-386
2006
Escherichia coli
Amundsen, S.K.; Taylor, A.F.; Reddy, M.; Smith, G.R.
Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots
Genes Dev.
21
3296-3307
2007
Escherichia coli
Amundsen, S.K.; Smith, G.R.
Chi hotspot activity in Escherichia coli without RecBCD exonuclease activity: implications for the mechanism of recombination
Genetics
175
41-54
2007
Escherichia coli
Ghatak, A.; Julin, D.A.
Kinetics of ATP-stimulated nuclease activity of the Escherichia coli RecBCD enzyme
J. Mol. Biol.
361
954-968
2006
Escherichia coli
Wong, C.J.; Rice, R.L.; Baker, N.A.; Ju, T.; Lohman, T.M.
Probing 3-ssDNA loop formation in E. coli RecBCD/RecBC-DNA complexes using non-natural DNA: a model for "Chi" recognition complexes
J. Mol. Biol.
362
26-43
2006
Escherichia coli (P08394 and P04993 and P07648), Escherichia coli
Handa, N.; Kowalczykowski, S.C.
A RecA mutant, RecA(730), suppresses the recombination deficiency of the RecBC(1004)D-chi* interaction in vitro and in vivo
J. Mol. Biol.
365
1314-1325
2007
Escherichia coli
Datta, S.; Costantino, N.; Zhou, X.; Court, D.L.
Identification and analysis of recombineering functions from Gram-negative and Gram-positive bacteria and their phages
Proc. Natl. Acad. Sci. USA
105
1626-1631
2008
Escherichia coli
Seki, E.; Matsuda, N.; Yokoyama, S.; Kigawa, T.
Cell-free protein synthesis system from Escherichia coli cells cultured at decreased temperatures improves productivity by decreasing DNA template degradation
Anal. Biochem.
377
156-161
2008
Escherichia coli
Roberts, G.; Cooper, L.; White, J.; Su, T.; Zipprich, J.; Geary, P.; Kennedy, C.; Dryden, D.
An investigation of the structural requirements for ATP hydrolysis and DNA cleavage by the EcoKI type I DNA restriction and modification enzyme
Nucleic Acids Res.
39
7667-7676
2011
Escherichia coli, Escherichia coli JM109
Choi, W.; Jang, S.; Harshey, R.
Mu transpososome and RecBCD nuclease collaborate in the repair of simple Mu insertions
Proc. Natl. Acad. Sci. USA
111
14112-14117
2014
Escherichia coli
Leung, W.Y.; Chung, L.H.; Kava, H.W.; Murray, V.
RecBCD (exonuclease V) is inhibited by DNA adducts produced by cisplatin and ultraviolet light
Biochem. Biophys. Res. Commun.
495
666-671
2018
Escherichia coli (P08394 AND P07648 AND P04993)
Wilkinson, M.; Chaban, Y.; Wigley, D.B.
Mechanism for nuclease regulation in RecBCD
eLife
5
e18227
2016
Escherichia coli (P08394 AND P07648 AND P04993)
EXTERNAL LINKS (specific for EC-Number 3.1.11.5)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
