Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme

scientific article published on 22 October 2004

Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1093/NAR/GKH899
P932PMC publication ID528788
P698PubMed publication ID15501920
P5875ResearchGate publication ID8215023

P2093author name stringDesirazu N Rao
Nidhanapati K Raghavendra
P2860cites workNucleoside triphosphate-dependent restriction enzymesQ24555228
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Q25938983
Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I.Q31937862
Model for how type I restriction enzymes select cleavage sites in DNA.Q33584495
ATP-dependent restriction enzymesQ33851803
Repressor induced site-specific binding of HU for transcriptional regulationQ33886892
DNA translocation blockage, a general mechanism of cleavage site selection by type I restriction enzymesQ33890885
Self-generated DNA termini relax the specificity of SgrAI restriction endonucleaseQ34008473
Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymesQ34358530
Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysisQ37698719
Functional cooperation between exonucleases and endonucleases--basis for the evolution of restriction enzymesQ39744399
Purification and properties of the P15 specific restriction endonuclease from Escherichia coliQ39799531
DNA communications by Type III restriction endonucleases--confirmation of 1D translocation over 3D loopingQ39946292
DNA recognition and cleavage by the EcoP15 restriction endonucleaseQ40289784
Endonuclease (R) subunits of type-I and type-III restriction-modification enzymes contain a helicase-like domainQ41131058
DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sitesQ43749963
S-Adenosyl Methionine Prevents Promiscuous DNA Cleavage by the EcoP1I type III Restriction EnzymeQ44608364
Scanning force microscopy of DNA translocation by the Type III restriction enzyme EcoP15I.Q52943618
Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavageQ55043499
DNA translocation by the restriction enzyme from E. coli KQ72855531
Purification of Lac repressor protein using polymer displacement and immobilization of the proteinQ73724694
P433issue19
P304page(s)5703-5711
P577publication date2004-10-22
P1433published inNucleic Acids ResearchQ135122
P1476titleUnidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme
P478volume32

Reverse relations

cites work (P2860)
Q24816456Characterization of the Type III restriction endonuclease PstII from Providencia stuartii.
Q37808061Conflicts targeting epigenetic systems and their resolution by cell death: novel concepts for methyl-specific and other restriction systems
Q35259150DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.
Q42002446DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
Q37839479DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements
Q42264175Dissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity
Q30479841Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping
Q37713815Maintaining a sense of direction during long-range communication on DNA.
Q34598959MmeI: a minimal Type II restriction-modification system that only modifies one DNA strand for host protection
Q40354195Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes
Q42128175S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI
Q64389526Single-site DNA cleavage by Type III restriction endonuclease requires a site-bound enzyme and a trans-acting enzyme that are ATPase-activated
Q37252417Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering.
Q42957729The single polypeptide restriction-modification enzyme LlaGI is a self-contained molecular motor that translocates DNA loops
Q34172705Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
Q42131651Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity
Q30494970Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat
Q37078204Type III restriction enzymes communicate in 1D without looping between their target sites
Q34358103Type III restriction-modification enzymes: a historical perspective

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