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Information on EC 3.1.21.5 - type III site-specific deoxyribonuclease
for references in articles please use BRENDA:EC3.1.21.5
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
3.1.21.5 type III site-specific deoxyribonuclease
IUBMB Comments
This is a large group of enzymes which, together with those now listed as EC 3.1.21.3 (type I site-specific deoxyribonuclease) and EC 3.1.21.4 (type II site-specific deoxyribonuclease), were previously listed separately in sub-subclasses EC 3.1.23 and EC 3.1.24. They have an absolute requirement for ATP but do not hydrolyse it; S-adenosy-L-methionine stimulates the reaction, but is not absolutely required. They recognize specific, short DNA sequences and cleave a short distance away from the recognition sequence. These enzymes exist as complexes with enzymes of similar specificity listed under EC 2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)] or EC 2.1.1.37 [DNA (cytosine-5-)-methyltransferase].
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showendonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Synonyms
ecop1, bsahi, type iii restriction enzyme, ecopi, ecop15, stylti, pstii, type iii restriction-modification system, type iii restriction endonuclease, llafi, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BsaHI
cj0031
EC 3.1.23
-
-
-
-
EC 3.1.24
-
-
-
-
Eco86II
EcoP1
EcoP15
EcoP15I
EcoPI
MmyCI
PspGI
-
recognizes the sequence CCWGG where W is A or T and cuts DNA before the first C in the cognate sequence
PstII
R.MmyCI
restriction endonuclease PstII
restriction-modification system
-
-
-
-
StyLTI
type III R-M enzyme
type III restriction endonuclease
type III restriction enzyme
type III restriction-modification enzyme
type III restriction-modification system
additional information
EcoP15I
-
-
type III restriction enzyme
-
-
-
-
type III restriction-modification enzyme
-
-
additional information
-
a complete listing of all these enzymes and their recognition sites has been produced by R.J. Roberts, this list is updated annually
additional information
-
a complete listing of all these enzymes and their recognition sites has been produced by R.J. Roberts, this list is updated annually
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
-
-
-
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
mechanism, model of DNA translocation and cleavage, overview
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
mechanism, formation of loop structures and DNA translocation
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
mechanism
prophage P1
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9075-08-5
not distinguished from EC 3.1.21.4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
Substrates: single-site cleavage is solely a result of the interaction between two independent enzymes: a cis-acting enzyme which is bound to its recognition site in the DNA and a trans-acting enzyme either bound to or activated by its substrate in ATP-dependent manner. The two cooperating enzymes in solution can come together via diffusion. For cleavage to happen, the interaction between the two nucleases should occur within a time period shorter than the time required by the enzyme in cis to leave its recognition site. In case of EcoP15I, this time is measured to be about 6-17 seconds. According to a model of DNA cleavage a recognition site bound Type III RM enzyme would undergo a conformational change induced by the hydrolysis of ATP making it both diffusion-competent and nucleolytically active. The activated nuclease can catalyze single-strand scission only in cooperation with another ATP-activated nuclease. It is proposed that this model is valid for both single-site and two-site cleavage, except that in single-site cleavage the cooperating nucleases come together by 3D diffusion, and in two-site cleavage they converge by 1D diffusion and/or looping
Products: -
Products: -
?
phage lambda DNA + H2O
?
Substrates: restriction activity requires the presence of both the restriction modification endonuclease protein and the methylase protein of the NgoAXP restriction modification system
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: EcoP15 recognizes nonpalindromic DNA sequences, it requires a pair of nonmethylated inversely orientated recognition sites
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?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the enzyme posseses helicase activity which may be involved in local unwinding of DNA in the cleavage sites
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: R.EcoPI has no strand separation activity
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: EcoP15 restriction is a very fast reaction that requires two unmodified recognition sites in inverted orientation. EcoP15 methylation is a slower reaction and is independent of the orientation of the sites
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: recognizes nonsymetric nucleotide sequences. A necessary condition for DNA cleavage is the presence of two unmethylated recognition sites which are inversely, head-to-head, oriented in the DNA double strand. A DNA substrate possessing one EcoP1 and one EcoP15 site in the head to head configuration can not be cleaved by an individual enzyme, however it is specifically digested in the simultaneously presence of both enzymes. The two different type III enzymes can functionally cooperate in the cleavage of DNA
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?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: restriction requires a pair of unmethylated, inversely oriented recognition sites. Suicidal restriction by EcoP15I is prevented if all the unmodified sites are in the same orientation. EcoP15I possesses an intrisic ATPase activity, the potential driving force of DNA translocation. The ATPase is recognition site-specific
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: action of type III restriction enzymes takes place on replicated or replicating DNA in VIVO and leaves daughter DNAs with breaks at nonallelic sites, that bacteriophage-mediated homologous recombinantion reconstitutes an intact DNA from them, and that REcBCD exonuclease blocks this repair by degradation from the restriction breaks
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: cleavage site does not depend on the sequence context of the recognition sie. The enzyme can cleave linear DNA having either recognition sites in the same orientation or a single recognition site. Cleavage occurs predominantly at a site proximal to the DNA end in the case of multiple site substrates. The mechanism requires two enzyme molecules cooperating to elicit double-stranded break on DNA. The enzyme translocates on DNA in a 5' to 3' direction from its recognition site, switch in the direction of enzyme motion at the FNA ends
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?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: communication between type III recognition sites by energy-dependent 1D translocation and not by thermally driven 3D looping
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: ECoP15I recognizes the non-symmetric DNA sequence 5'-CAGCAG. For efficient cleavage, the enzyme needs the interaction with two copies of the recognition sequence that have to be inversely oriented in the DNA double-strand. The enzyme cuts the upper DNA strand 25-26 bp and the lower DNA strand 27-28 bp, respectively, downstream of the recognition sequence
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?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: EcoP15I rrequires the interaction with two inversely oriented 5'-CAGCAG recognition sites for efficient DNA cleavage
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: type III REs require two copies of their asymmetric recognition site in an indirectly repeated, head-to-head orientation cleaving the DNA 25-27 bp downstream of only one of the two sites
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
Substrates: the kinetics of ATP hydrolysis by EcoP15I is influenced by the proximity of DNA ends to the site. DNA cleavage by the Type III restriction enzymes requires long-range protein communication between recognition sites facilitated by thermally-driven 1D diffusion. This DNA sliding is initiated by hydrolysis of multiple ATPs catalysed by a helicase-like domain. Two distinct ATPase phases are observed using short oligoduplex substrates; the rapid consumption of about 10 ATPs coupled to a protein conformation switch followed by a slower phase, the duration of which is dictated by the rate of dissociation from the recognition site. The second ATPase phase is both variable and only observable when DNA ends are proximal to the recognition site. On DNA with sites more distant from the ends, a single ATPase phase coupled to the conformation switch is observed and subsequent site dissociation requires little or no further ATP hydrolysis. The overall DNA dissociation kinetics (encompassing site release, DNA sliding and escape via a DNA end) are not influenced by the second phase
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
Substrates: BsaHI recognises a palindromic sequence of bases and cleaves within this sequence between the purine and cytosine bases: GR/CGYC
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: BsaHI recognises a palindromic sequence of bases and cleaves within this sequence between the purine and cytosine bases: GR/CGYC
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CGAAT-3'
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-GCAG-3'
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Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CCACC-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: recognition sequence: CTGATG. The enzyme requires a substrate with two copies of the recognition site in head-to-head repeat and is dependent on a low level of ATP hydrolysis (about 40 ATP/site/min). PstII can cut DNA with GTP and CTP
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CATCAG-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: recognition sequence: CTGATG. The enzyme requires a substrate with two copies of the recognition site in head-to-head repeat and is dependent on a low level of ATP hydrolysis (about 40 ATP/site/min). PstII can cut DNA with GTP and CTP
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
Substrates: DNA cleavage by the Type III restriction enzymes requires long-range protein communication between recognition sites facilitated by thermally-driven 1D diffusion. This DNA sliding is initiated by hydrolysis of multiple ATPs catalysed by a helicase-like domain. Two distinct ATPase phases are observed using short oligoduplex substrates; the rapid consumption of about 10 ATPs coupled to a protein conformation switch followed by a slower phase, the duration of which is dictated by the rate of dissociation from the recognition site. The second ATPase phase is both variable and only observable when DNA ends are proximal to the recognition site. On DNA with sites more distant from the ends, a single ATPase phase coupled to the conformation switch is observed and subsequent site dissociation requires little or no further ATP hydrolysis. The overall DNA dissociation kinetics (encompassing site release, DNA sliding and escape via a DNA end) are not influenced by the second phase
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CAGAG-3'
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleavage also occurs for two adjacent head to head and tail to tail oriented target sites, but only at one of the two possible sites, DNA translocation is not required
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Products: -
?
additional information
?
-
-
Substrates: cooperation of enzyme with EcoP15I in DNa cleavage, cleavage predominantly at EcoP15I site, EcpP1I greatly stimulates EcoP15I nicking activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural requirements of substrate, overview
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Products: -
?
additional information
?
-
-
Substrates: the database REBASE contains information about recognition sites and cleavage sites
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Products: -
?
additional information
?
-
-
Substrates: the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites
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?
additional information
?
-
-
Substrates: the pre-incubation of EcoP15I with DNA has no significant influence on the enzyme's ability to cleave DNA
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Products: -
?
additional information
?
-
-
Substrates: on linear DNA in contrast, there is only one route and resolvase completely blocks communication and cleavage, while on circular DNA, there are two routes for communication. If one route is blocked by resolvase, the enzyme can use the alternative route. No stepwise motor mechanism for type III enzymes, the enzyme can bypass triplexes during sliding
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?
additional information
?
-
-
Substrates: EcoP15I recognizes 5'-CAGCAG-3' as target site. Cleavage occurs at a defined location next to only one of the sites, and one of the two sites is chosen for cleavage randomly, although this is influenced by the base composition of the DNA. The EcoP15I R/M enzyme cuts the sequence CAGCAG(N)25/27 as long as the underlined adenine is unmethylated. Preference for a two-site substrate. ATP hydrolysis is essential for the overall restriction process
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Products: -
?
additional information
?
-
-
Substrates: DNA end capping stimulates cleavage of tail-to-tail oriented pairs of sites, rates of cleavage of tail-to-tail repeats, ATP hydrolysis rates, and DNA cleavage kinetics, overview
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Products: -
?
additional information
?
-
-
Substrates: EcoP15I that hydrolyses many ATPs upon initiation
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?
additional information
?
-
-
Substrates: type III restriction endonucleases comprise of one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
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?
additional information
?
-
-
Substrates: the recognition motif is GAGCC, with the first cytosine base being methylated by the ECo86II restriction-modification system. The site of cutting maps to approximately 25 bp 3' to the GAGCC Eco86II recognition sites
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-
additional information
?
-
Escherichia coli NT86
-
Substrates: the recognition motif is GAGCC, with the first cytosine base being methylated by the ECo86II restriction-modification system. The site of cutting maps to approximately 25 bp 3' to the GAGCC Eco86II recognition sites
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Products: -
-
additional information
?
-
-
Substrates: type III restriction-modification systems play only a minor role in the overall defence of the cell against invasion by foreign DNA
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Products: -
?
additional information
?
-
-
Substrates: the methyltransferase (modification) subunit of MmyCI recognizes the sequence 5'-TGAG-3' and methylates the adenine
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Products: -
?
additional information
?
-
-
Substrates: the methyltransferase (modification) subunit of MmyCI recognizes the sequence 5'-TGAG-3' and methylates the adenine
Products: -
Products: -
?
additional information
?
-
prophage P1
-
Substrates: cleavage generally depends on ratio of enzyme to cleavage sites, in presence of S-adenosyl-L-methionine, substrates with two cleavage sites in inverted repeats are susceptible, in absence of S-adenosyl-L-methionine, presence of Na+ leads to cleavage only in substrates with two sites in inverted repeats, presence of K+ leads to cleavage of all substrates
Products: -
Products: -
?
additional information
?
-
prophage P1
-
Substrates: cooperation of enzyme with EcoP1I in DNa cleavage, cleavage predominantly at EcoP15I site, EcoP1I greatly stimulates EcoP15I nicking activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: type III restriction endonucleases comprise of one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: action of type III restriction enzymes takes place on replicated or replicating DNA in VIVO and leaves daughter DNAs with breaks at nonallelic sites, that bacteriophage-mediated homologous recombinantion reconstitutes an intact DNA from them, and that REcBCD exonuclease blocks this repair by degradation from the restriction breaks
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CGAAT-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-GCAG-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CCACC-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CATCAG-3'
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
Products: -
Products: -
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
Substrates: the recognition sequence is 5'-CAGAG-3'
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: on linear DNA in contrast, there is only one route and resolvase completely blocks communication and cleavage, while on circular DNA, there are two routes for communication. If one route is blocked by resolvase, the enzyme can use the alternative route. No stepwise motor mechanism for type III enzymes, the enzyme can bypass triplexes during sliding
Products: -
Products: -
?
additional information
?
-
-
Substrates: type III restriction-modification systems play only a minor role in the overall defence of the cell against invasion by foreign DNA
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
-
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage
ATP
DNA cleavage by the Type III restriction enzymes requires long-range protein communication between recognition sites facilitated by thermally-driven 1D diffusion. This DNA sliding is initiated by hydrolysis of multiple ATPs catalysed by a helicase-like domain. Two distinct ATPase phases are observed using short oligoduplex substrates; the rapid consumption of about 10 ATPs coupled to a protein conformation switch followed by a slower phase, the duration of which is dictated by the rate of dissociation from the recognition site. The second ATPase phase is both variable and only observable when DNA ends are proximal to the recognition site. On DNA with sites more distant from the ends, a single ATPase phase coupled to the conformation switch is observed and subsequent site dissociation requires little or no further ATP hydrolysis. The overall DNA dissociation kinetics (encompassing site release, DNA sliding and escape via a DNA end) are not influenced by the second phase
ATP
DNA cleavage by the Type III restriction enzymes requires long-range protein communication between recognition sites facilitated by thermally-driven 1D diffusion. This DNA sliding is initiated by hydrolysis of multiple ATPs catalysed by a helicase-like domain. Two distinct ATPase phases are observed using short oligoduplex substrates; the rapid consumption of about 10 ATPs coupled to a protein conformation switch followed by a slower phase, the duration of which is dictated by the rate of dissociation from the recognition site. The second ATPase phase is both variable and only observable when DNA ends are proximal to the recognition site. On DNA with sites more distant from the ends, a single ATPase phase coupled to the conformation switch is observed and subsequent site dissociation requires little or no further ATP hydrolysis. The overall DNA dissociation kinetics (encompassing site release, DNA sliding and escape via a DNA end) are not influenced by the second phase
S-adenosyl-L-methionine
prophage P1
-
allosteric activator and specificity factor that ensures that cleavage only occurs when two endonucleases bind two recognition sites in a designated orientation
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine is not necessary for DNA cleavage, the presence of S-adenosyl-L-methionine dramatically impaires DNA cleavage due to competing DNA methylation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HU protein
-
binding of HU protein interfers with R.EcoP15I cleavage activity
-
Lac repressor
-
cleavage can be abolished by the binding of Lac repressor downstream (3' side) but not upstream (5' side) of the recognition site
-
additional information
-
type III restriction is alleviated by bacteriophage (RecE) homologous recombination function
-
additional information
-
sinefungin neither has an appreciable effect on DNA cleavage by EcoP15I nor compensated for the second recognition site; the catalytic activity of EcoP15I after 3 h of pre-incubation without DNA is strongly decreased
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N4-adenosyl-N4-methyl-2,4-diaminobutanoic acid
-
may substitute for S-adenosyl-L-methionine
additional information
-
type III restriction is enhanced by bacterial (RecBCD) function
-
ATP
-
ATP hydrolysis activated by recognition site binding leads to release of the enzyme from the site, dissociation from the substrate via a free DNA end and cleavage of the DNA
ATP
-
ATP hydrolysis activated by recognition site binding leads to release of the enzyme from the site, dissociation from the substrate via a free DNA end and cleavage of the DNA
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Myopia, Degenerative
[Studies of the association of pathological myopia in Chinese patients with HLA alleles]
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
the optimal temperature for DNA cleavage by PspGI is at 80°C or above
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
motile but non-swarming variant 11168 and a chicken-adapted hypermotile variant CH11168
UniProt
brenda
motile but non-swarming variant 11168 and a chicken-adapted hypermotile variant CH11168
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
DNA cleavage by the type III restriction-modification enzymes requires communication in 1D between two distant indirectly-repeated recognitions sites, resulting in non-specific dsDNA cleavage close to only one of the two sites. The cleavage site selection reflects the dynamics of the preceding stochastic enzyme events that are consistent with bidirectional motion in 1D and DNA cleavage following head-on protein collision. The type III REs exhibits site orientation selectivity
physiological function
-
characterization of a type III-like restriction system present in clinical Staphylococcus aureus strains that prevents transformation with DNA from other bacterial species. Some methicillin-resistant strains are deficient in this restriction system, and thus are hypersusceptible to the horizontal transfer of DNA from other species, such as Escherichia coli, and could easily acquire a vancomycin-resistance gene from Enterococci, overview
physiological function
dual role for phase variation of the enzyme as a limiter of phage spread and a regulator of a gene expression. The underlying mechanism of action for the alteration in gene expression is not known and does not appear to involve differential methylation of specific recognition sites by Cj0031. Phase variation of Cj0031, as detected during infections in chickens and mice, produces changes in expression of multiple genes that may lead to phenotypic variation and generation of highly differentiated variants with differing capabilities of adaptation to diverse niches
physiological function
Type III RM enzymes are bacterial defense systems that protect the host from invading foreign DNA by nucleolytically cleaving them at specific recognition sites
physiological function
-
dual role for phase variation of the enzyme as a limiter of phage spread and a regulator of a gene expression. The underlying mechanism of action for the alteration in gene expression is not known and does not appear to involve differential methylation of specific recognition sites by Cj0031. Phase variation of Cj0031, as detected during infections in chickens and mice, produces changes in expression of multiple genes that may lead to phenotypic variation and generation of highly differentiated variants with differing capabilities of adaptation to diverse niches
-
additional information
-
sliding model for long-range communication on DNA by type III restriction enzymes, distribution of cleavage on head-to-head substrates with end bias, overview
additional information
-
several models for the mode of action of type III R/M enzymes, detailed overview. 1. Translocation, loop extrusion and collision model. 2. The end reversal model. 3. Transient looping and translocation model from atomic force spectroscopy
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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). T3RE_BACC1
Bacillus cereus (strain ATCC 10987 / NRS 248)
987
0
114787
Swiss-Prot
other Location (Reliability: 2)
T3RE_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
990
0
113388
Swiss-Prot
Mitochondrion (Reliability: 3)
T3RH_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
514
1
59880
Swiss-Prot
-
CAS10_THEON
Thermococcus onnurineus (strain NA1)
777
0
88009
Swiss-Prot
-
Q0PC94_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
1243
0
146452
TrEMBL
-
Q5F957_NEIG1
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
979
0
111427
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
106000
-
x * 106000, subunit Res, + x * 75000, subunit Mod, deduced from gene sequence
110957
-
1 * 110957 + 2 * 74094, EcoP15I, calculated from amino acid sequence
74000
74094
-
1 * 110957 + 2 * 74094, EcoP15I, calculated from amino acid sequence
75000
-
x * 106000, subunit Res, + x * 75000, subunit Mod, deduced from gene sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 106000, subunit Res, + x * 75000, subunit Mod, deduced from gene sequence
heterotrimer
tetramer
additional information
heterotrimer
-
1 * 110957 + 2 * 74094, EcoP15I, calculated from amino acid sequence
heterotrimer
-
1 * 111459 + 2 * 73486, EcoPI, calculated from amino acid sequence
heterotrimer
-
1 * 108264 + 2 * 63715, calculated from amino acid sequence
tetramer
-
the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
tetramer
-
the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo
-
additional information
-
functional interaction of enzymes EcoP1I and EcoP15I
additional information
-
separation of Res and Mod subunits by gel filtration in presence of 2 M NaCl
additional information
-
in the presence of specific DNA, the entire modification subunit of the enzyme is protected from trypsin digestion, whereas in the absence of DNA stable protein domains of the modification subunit are not detected. In contrast, the restriction subunit is comprised of two trypsin-resistant domains of about 77000-79000 Da and 27000-29000 Da, respectively. Both structural restriction domains are connected by a flexible linker region that spans 23 amino acid residues
additional information
-
the type III R/M enzymes comprise two modification subunits, each containing a target recognition domain to bind to the target sequence and a methyltransferase catalytic domain to monitor the methylation status of an adenine in the target, and two restriction subunits each containing a DNA helicase and ATP-hydrolysing domain and an endonuclease DNA cleavage domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
real-time imaging of enzyme at scan rates of 1-3 frames per s. EcoP15I translocates DNA in an ATP-dependent manner, at a rate of 79 bp/s, resulting in the accumulation of supercoiling. EcoP15I bound to its recognition site also makes nonspecific contacts with other DNA sites, thus forming DNA loops and reducing the distance between the two recognition sites
-
study of enzyme-DNA pre-cleavage complexes by atomic force microscopy. DNA loops observed are formed by a contact between site-bound EcoP15I enzyme and a nonspecific region of DNA, and do not result from translocation. Model for restricition by type III enzymes involving both structural elements, and a functional reason for the unusual site orientation required for the cleavage reaction
-
cryo-EM structures of Csm-crRNA binary, as well as Csm-crRNA-target RNA and Csm-crRNA-target RNAanti-tag ternary complexes at an average resolution of 3.0 A, 3.1 A and 3.1 A, respectively. The five proteins of the Csm complex are assembled with crRNA into an intertwined helical topology. The topology of the 5'-repeat tag is important for avoidance of autoimmunity, and an autoinhibitory loop controls target RNA-mediated DNase cleavage activity by the HD domain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G448S
-
mutant of Mod subunit, not able to bind S-adenosyl-L-methionine, no DNA cleavage
D354A
mutant shows reduced activity compared to the wild type enzyme
E350A
mutant shows reduced activity compared to the wild type enzyme
F353A
mutant shows reduced activity compared to the wild type enzyme
P349A
mutant shows reduced activity compared to the wild type enzyme
Q344A
mutant shows activity similar to wild type enzyme
R352A
mutant shows activity similar to the wild type enzyme
S348A
mutant shows activity similar to the wild type enzyme
F353A
-
mutant shows reduced activity compared to the wild type enzyme
-
P349A
-
mutant shows reduced activity compared to the wild type enzyme
-
R352A
-
mutant shows activity similar to the wild type enzyme
-
S348A
-
mutant shows activity similar to the wild type enzyme
-
additional information
additional information
-
mutant c2-134, unable to cleave DNA, mutant c2-440, poor ability to cleave DNA
additional information
-
study on the predicted linker region between the two domains of the restriction subunit by insertional mutagenesis. Introduction of up to 18 amino acids in the N- and C-terminal region of the linker. The region tolerated the introduced genetic alterations without loss of catalytic function or changes in cleavage position
additional information
-
analysis of several strains for phase variable methyltransferase activity, mod, and restriction endonuclease activity. Of 41 strains in the survey that contain a phase variable mod gene, seven have an obvious mutation in the restriction domain and appear to be dedicated phasevarions. The remaining 15 strains that do not contain a phase variable mod gene are likely to be dedicated, functional, type III restriction-modification systems
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Csm1-Csm4 subcomplex, Csm2, Csm3 and Csm5 in the Csm CRISPR-Cas locus are respectively expressed in Escherichia coli and assembled with crRNA in vitro at a molar ratio of 1:1.5:4:1.5:1.3. Formation of a homogeneous complex containing all bound Csm subunits only occurs in the presence of crRNA
partial purification by ion exchange/affinity chromatography over a Heparin column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into pQE-16 plasmid vector that provides the enzyme with a C-terminal 6His-tag
-
expression in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of separated Res and Mod subunits leads to an inactive apoenzyme lacking S-adenosyl-L-methionine, reconstitution in presence of S-adenosyl L-methionine was not successful
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
inactivation of this restriction system dramatically increases the transformation efficiency of clinical Staphylococcus aureus methicillin-resistant strains, opening the field of molecular genetic manipulation of these strains using DNA of exogenous origin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roberts, R.J.
Restriction enzymes and their isoschizomers
Nucleic Acids Res.
18
2331-2365
1990
Escherichia coli, Haemophilus influenzae, Salmonella enterica subsp. enterica serovar Typhi
brenda
Roberts, R.J.
Restriction and modification enzymes and their recognition sequences
Nucleic Acids Res.
11
r135-r167
1983
Escherichia coli
brenda
Roberts, R.J.; Macelis, D.
REBASE - restriction enzymes and methylases
Nucleic Acids Res.
29
268-269
2001
Escherichia coli
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Kruger, D.H.; Kupper, D.; Meisel, A.; Tierlich, M.; Reuter, M.; Schroeder, C.
Restriction endonucleases functionally interacting with two DNA sites
Gene
157
165
1995
Escherichia coli
brenda
Gorbalenya, A.E.; Koonin, E.V.
Endonuclease (R) subunit of type-I and type-III restriction-modification enzymes contain a helicase-like domain
FEBS Lett.
291
277-281
1991
Escherichia coli
brenda
Kunz, A.; Mackeldanz, P.; Mucke, M.; Meisel, A.; Reuter, M.; Schroeder, C.; Kruger, D.H.
Mutual activation of two restriction endonucleases: interaction of EcoP1 and EcoP15
Biol. Chem.
379
617-620
1998
Escherichia coli
brenda
Su, P.; Im, H.; Hsieh, H.; Kang'a, S.; Dunn, N.W.
LlaFI, a type III restriction and modification system in Lactococcus lactis
Appl. Environ. Microbiol.
65
686-693
1999
Lactococcus lactis
brenda
Meisel, A.; Bickle, T.A.; Kruger, T.A.; Kruger, D.H.; Schroeder, C.
Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
Nature
355
467-469
1992
Escherichia coli
brenda
Meisel, A.; Mackeldanz, P.; Bickle, T.A.; Kruger, D.H.; Schroeder, C.
Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis
EMBO J.
14
2958-2966
1995
Escherichia coli
brenda
Saha, S.; Rao, D.N.
Mutations in the Res subunit of the EcoPI restriction enzyme that affect ATP-dependent reactions
J. Mol. Biol.
269
342-354
1997
Escherichia coli
brenda
Hegna, I.K.; Bratland, H.; Kolsto, A.B.
BceS1, a new addition to the type III restriction and modification family
FEMS Microbiol. Lett.
202
189-193
2001
Bacillus cereus (P25241)
brenda
Janscak, P.; Sandmeier, U.; Szczelkun, M.D.; Bickle, T.A.
Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I
J. Mol. Biol.
306
417-431
2001
Escherichia coli, prophage P1
brenda
Bist, P.; Sistla, S.; Krishnamurthy, V.; Acharya, A.; Chandrakala, B.; Rao, D.N.
S-adenosyl-L-methionine is required for DNA cleavage by type III restriction enzymes
J. Mol. Biol.
310
93-109
2001
Escherichia coli
brenda
Mucke, M.; Reich, S.; Moncke-Buchner, E.; Reuter, M.; Kruger, D.H.
DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites
J. Mol. Biol.
312
687-698
2001
Escherichia coli
brenda
Peakman, L.J.; Antognozzi, M.; Bickle, T.A.; Janscak, P.; Szczelkun, M.D.
S-adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme
J. Mol. Biol.
333
321-335
2003
prophage P1
brenda
Reich, S.; Gossl, I.; Reuter, M.; Rabe, J.P.; Kruger, D.H.
Scanning force microscopy of DNA translocation by the type III restriction enzyme EcoP15I
J. Mol. Biol.
341
337-343
2004
Escherichia coli
brenda
Dryden, D.T.; Murray, N.E.; Rao, D.N.
Nucleoside triphosphate-dependent restriction enzymes
Nucleic Acids Res.
29
3728-3741
2001
Escherichia coli
brenda
Handa, N.; Kobayashi, I.
Type III restriction is alleviated by bacteriophage (RecE) homologous recombination function but enhanced by bacterial (RecBCD) function
J. Bacteriol.
187
7362-7373
2005
Escherichia coli
brenda
Mncke-Buchner, E.; Mackeldanz, P.; Kruger, D.H.; Reuter, M.
Overexpression and affinity chromatography purification of the Type III restriction endonuclease EcoP15I for use in transcriptome analysis
J. Biotechnol.
114
99-106
2004
Escherichia coli
brenda
Peakman, L.J.; Szczelkun, M.D.
DNA communications by Type III restriction endonucleases--confirmation of 1D translocation over 3D looping
Nucleic Acids Res.
32
4166-4174
2004
Escherichia coli
brenda
Raghavendra, N.K.; Rao, D.N.
Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme
Nucleic Acids Res.
32
5703-5711
2004
Escherichia coli
brenda
Sears, A.; Szczelkun, M.D.
Subunit assembly modulates the activities of the Type III restriction-modification enzyme PstII in vitro
Nucleic Acids Res.
33
4788-4796
2005
Providencia stuartii, Providencia stuartii 164
brenda
Crampton, N.; Roes, S.; Dryden, D.T.; Rao, D.N.; Edwardson, J.M.; Henderson, R.M.
DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
EMBO J.
26
3815-3825
2007
Escherichia coli, Escherichia coli P15I
brenda
Wagenfuehr, K.; Pieper, S.; Mackeldanz, P.; Linscheid, M.; Krueger, D.H.; Reuter, M.
Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis
J. Mol. Biol.
366
93-102
2007
Escherichia coli
brenda
Fox, K.L.; Dowideit, S.J.; Erwin, A.L.; Srikhanta, Y.N.; Smith, A.L.; Jennings, M.P.
Haemophilus influenzae phasevarions have evolved from type III DNA restriction systems into epigenetic regulators of gene expression
Nucleic Acids Res.
35
5242-5252
2007
Haemophilus influenzae
brenda
Crampton, N.; Yokokawa, M.; Dryden, D.T.; Edwardson, J.M.; Rao, D.N.; Takeyasu, K.; Yoshimura, S.H.; Henderson, R.M.
Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping
Proc. Natl. Acad. Sci. USA
104
12755-12760
2007
Escherichia coli
brenda
Neely, R.K.; Roberts, R.J.
The BsaHI restriction-modification system: cloning, sequencing and analysis of conserved motifs
BMC Mol. Biol.
9
48
2008
Geobacillus stearothermophilus (B0LX59)
brenda
Moencke-Buchner, E.; Rothenberg, M.; Reich, S.; Wagenfuehr, K.; Matsumura, H.; Terauchi, R.; Krueger, D.H.; Reuter, M.
Functional characterization and modulation of the DNA cleavage efficiency of type III restriction endonuclease EcoP15I in its interaction with two sites in the DNA target
J. Mol. Biol.
387
1309-1319
2009
Escherichia coli
brenda
Carpenter, M.A.; Bhagwat, A.S.
DNA base flipping by both members of the PspGI restriction-modification system
Nucleic Acids Res.
36
5417-5425
2008
Pyrococcus sp. GI-H
brenda
Ramanathan, S.P.; van Aelst, K.; Sears, A.; Peakman, L.J.; Diffin, F.M.; Szczelkun, M.D.; Seidel, R.
Type III restriction enzymes communicate in 1D without looping between their target sites
Proc. Natl. Acad. Sci. USA
106
1748-1753
2009
Escherichia coli
brenda
Adamczyk-Poplawska, M.; Lower, M.; Piekarowicz, A.
Characterization of the NgoAXP: phase-variable type III restriction-modification system in Neisseria gonorrhoeae
FEMS Microbiol. Lett.
300
25-35
2009
Neisseria gonorrhoeae (Q5F957), Neisseria gonorrhoeae
brenda
Schwarz, F.W.; van Aelst, K.; Toth, J.; Seidel, R.; Szczelkun, M.D.
DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion
Nucleic Acids Res.
39
8042-8051
2011
Escherichia coli
brenda
Corvaglia, A.R.; Francois, P.; Hernandez, D.; Perron, K.; Linder, P.; Schrenzel, J.
A type III-like restriction endonuclease functions as a major barrier to horizontal gene transfer in clinical Staphylococcus aureus strains
Proc. Natl. Acad. Sci. USA
107
11954-11958
2010
Escherichia coli, Staphylococcus aureus
brenda
Van Aelst, K.; Toth, J.; Ramanathan, S.; Schwarz, F.; Seidel, R.; Szczelkun, M.
Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat
Proc. Natl. Acad. Sci. USA
107
9123-9128
2010
Escherichia coli
brenda
Gupta, Y.K.; Yang, L.; Chan, S.H.; Samuelson, J.C.; Xu, S.Y.; Aggarwal, A.K.
Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering
J. Mol. Biol.
420
261-268
2012
Escherichia coli
brenda
Toth, J.; van Aelst, K.; Salmons, H.; Szczelkun, M.D.
Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity
Nucleic Acids Res.
40
6752-6764
2012
Escherichia coli
brenda
Rao, D.N.; Dryden, D.T.; Bheemanaik, S.
Type III restriction-modification enzymes: a historical perspective
Nucleic Acids Res.
42
45-55
2014
Providencia stuartii, Lactococcus lactis, Neisseria gonorrhoeae, Helicobacter pylori, Bacillus cereus, Mannheimia haemolytica, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Haemophilus influenzae, Escherichia coli 15T-
brenda
Butterer, A.; Pernstich, C.; Smith, R.M.; Sobott, F.; Szczelkun, M.D.; Toth, J.
Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
Nucleic Acids Res.
42
5139-5150
2014
Providencia stuartii, Escherichia coli
brenda
Algire, M.A.; Montague, M.G.; Vashee, S.; Lartigue, C.; Merryman, C.
A type III restriction-modification system in Mycoplasma mycoides subsp. capri
Open Biology
2
120115
2012
Mycoplasma mycoides subsp. capri, Mycoplasma mycoides subsp. capri GM12
brenda
Schwarz, F.W.; Toth, J.; van Aelst, K.; Cui, G.; Clausing, S.; Szczelkun, M.D.; Seidel, R.
The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA
Science
340
353-356
2013
Escherichia coli
brenda
Toth, J.; Bollins, J.; Szczelkun, M.D.
Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes
Nucleic Acids Res.
43
10870-10881
2015
Punavirus P1 (P08764), Escherichia coli (P12364)
brenda
Anjum, A.; Brathwaite, K.J.; Aidley, J.; Connerton, P.L.; Cummings, N.J.; Parkhill, J.; Connerton, I.; Bayliss, C.D.
Phase variation of a Type IIG restriction-modification enzyme alters site-specific methylation patterns and gene expression in Campylobacter jejuni strain NCTC11168
Nucleic Acids Res.
44
4581-4594
2016
Campylobacter jejuni (Q0PC94), Campylobacter jejuni NCTC 11168 (Q0PC94)
brenda
Ahmad, I.; Kulkarni, M.; Gopinath, A.; Saikrishnan, K.
Single-site DNA cleavage by Type III restriction endonuclease requires a site-bound enzyme and a trans-acting enzyme that are ATPase-activated
Nucleic Acids Res.
46
6229-6237
2018
Escherichia coli (Q5ZND2)
brenda
Jia, N.; Mo, C.; Wang, C.; Eng, E.; Marraffini, L.; Patel, D.
Type III-A CRISPR-Cas Csm complexes assembly, periodic RNA cleavage, DNase activity regulation, and autoimmunity
Mol. Cell.
73
264-277.e5
2019
Thermococcus onnurineus (B6YWB8)
brenda
Murray, I.; Luyten, Y.; Fomenkov, A.; Dai, N.; Correa, I.; Farmerie, W.; Clark, T.; Korlach, J.; Morgan, R.; Roberts, R.
Structural and functional diversity among type III restriction-modification systems that confer host DNA protection via methylation of the N4 atom of cytosine
PLoS ONE
16
e0253267
2021
Escherichia coli, Escherichia coli NT86
brenda
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