Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
about
SF1 and SF2 helicases: family mattersPhosphate and R2D2 restrict the substrate specificity of Dicer-2, an ATP-driven ribonucleaseEvolutionary Ecology of Prokaryotic Immune MechanismsThe structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction proteinType III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeatpHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I.Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA.Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleasesStructure and operation of the DNA-translocating type I DNA restriction enzymes.Sequence-specific assembly of FtsK hexamers establishes directional translocation on DNA.DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzymeProbing DNA helicase kinetics with temperature-controlled magnetic tweezersTranslocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA.Type III restriction enzymes communicate in 1D without looping between their target sites.Superfamily 2 helicasesSingle molecule studies of homologous recombination.Maintaining a sense of direction during long-range communication on DNA.DNA translocation by type III restriction enzymes: a comparison of current models of their operation derived from ensemble and single-molecule measurements.Diverse functions of restriction-modification systems in addition to cellular defenseType I restriction enzymes and their relatives.Recycling of protein subunits during DNA translocation and cleavage by Type I restriction-modification enzymes.CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNADissociation from DNA of Type III Restriction-Modification enzymes during helicase-dependent motion and following endonuclease activity.DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.The single polypeptide restriction-modification enzyme LlaGI is a self-contained molecular motor that translocates DNA loops.DNA cleavage and methylation specificity of the single polypeptide restriction-modification enzyme LlaGI.Fork sensing and strand switching control antagonistic activities of RecQ helicases.The interrelationship of helicase and nuclease domains during DNA translocation by the molecular motor EcoR124I.Catching DNA with hoops-biophysical approaches to clarify the mechanism of SMC proteins.The condensin complex is a mechanochemical motor that translocates along DNA.The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.
P2860
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P2860
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
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2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
name
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@ast
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@en
type
label
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@ast
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@en
prefLabel
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@ast
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.
@en
P2860
P356
P1433
P1476
Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I
@en
P2093
Joost G P Bloom
Ralf Seidel
P2860
P304
P356
10.1038/EMBOJ.2008.69
P407
P577
2008-04-03T00:00:00Z