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DNA + H2O
?
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
phage lambda DNA + H2O
?
restriction activity requires the presence of both the restriction modification endonuclease protein and the methylase protein of the NgoAXP restriction modification system
-
-
?
additional information
?
-
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
EcoP15 recognizes nonpalindromic DNA sequences, it requires a pair of nonmethylated inversely orientated recognition sites
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the enzyme posseses helicase activity which may be involved in local unwinding of DNA in the cleavage sites
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
R.EcoPI has no strand separation activity
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
communication between type III recognition sites by energy-dependent 1D translocation and not by thermally driven 3D looping
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
EcoP15I rrequires the interaction with two inversely oriented 5'-CAGCAG recognition sites for efficient DNA cleavage
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
BsaHI recognises a palindromic sequence of bases and cleaves within this sequence between the purine and cytosine bases: GR/CGYC
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
BsaHI recognises a palindromic sequence of bases and cleaves within this sequence between the purine and cytosine bases: GR/CGYC
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CGAAT-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-GCAG-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CCACC-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CATCAG-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
Punavirus P1
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CAGAG-3'
-
-
?
additional information
?
-
-
the database REBASE contains information about recognition sites and cleavage sites
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
cooperation of enzyme with EcoP15I in DNa cleavage, cleavage predominantly at EcoP15I site, EcpP1I greatly stimulates EcoP15I nicking activity
-
?
additional information
?
-
-
structural requirements of substrate, overview
-
?
additional information
?
-
-
the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites
-
-
?
additional information
?
-
-
the pre-incubation of EcoP15I with DNA has no significant influence on the enzyme's ability to cleave DNA
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
EcoP15I that hydrolyses many ATPs upon initiation
-
-
?
additional information
?
-
-
type III restriction endonucleases comprise of one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
-
-
?
additional information
?
-
-
type III restriction-modification systems play only a minor role in the overall defence of the cell against invasion by foreign DNA
-
-
?
additional information
?
-
-
the methyltransferase (modification) subunit of MmyCI recognizes the sequence 5'-TGAG-3' and methylates the adenine
-
-
?
additional information
?
-
-
the methyltransferase (modification) subunit of MmyCI recognizes the sequence 5'-TGAG-3' and methylates the adenine
-
-
?
additional information
?
-
prophage P1
-
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
-
?
additional information
?
-
prophage P1
-
cooperation of enzyme with EcoP1I in DNa cleavage, cleavage predominantly at EcoP15I site, EcoP1I greatly stimulates EcoP15I nicking activity
-
?
additional information
?
-
-
type III restriction endonucleases comprise of one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
additional information
?
-
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequences of EcoP15I and EcoPI are 5'-CAGCAG-3' and 5'-AGACC-3' , respectively'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CGAAT-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-GCAG-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CCACC-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
-
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CATCAG-3'
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
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
-
-
?
DNA + H2O
specific double-stranded DNA fragments with terminal 5'-phosphate
-
the recognition sequence is 5'-CAGAG-3'
-
-
?
additional information
?
-
-
the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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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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
brenda
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
Bacillus cereus, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Lactococcus lactis, Mannheimia haemolytica, Neisseria gonorrhoeae, Providencia stuartii, Salmonella enterica subsp. enterica serovar Typhimurium, 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
Escherichia coli, Providencia stuartii
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