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Results 1 - 10
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163
RecBCD Enzyme: Relationship of ATP Hydrolysis to the Unwinding of Duplex DNA+
, 1988
"... ABSTRACT: We find that the rate of dsDNA-dependent ATPase activity is biphasic, with a fast component which represents the unwinding of the dsDNA and a slow component which results from the ssDNA-dependent ATPase activity of recBCD enzyme. Comparison of the ATPase and helicase activities permits eva ..."
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ABSTRACT: We find that the rate of dsDNA-dependent ATPase activity is biphasic, with a fast component which represents the unwinding of the dsDNA and a slow component which results from the ssDNA-dependent ATPase activity of recBCD enzyme. Comparison of the ATPase and helicase activities permits
Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme
- J. Biol. Chem
, 2005
"... We recently demonstrated that the RecBCD enzyme is a bipolar DNA helicase that employs two single-stranded DNA motors of opposite polarity to drive translocation and unwinding of duplex DNA. We hypothesized that this organization may explain the exceptionally high rate and processivity of DNA unwind ..."
Abstract
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Cited by 11 (3 self)
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We recently demonstrated that the RecBCD enzyme is a bipolar DNA helicase that employs two single-stranded DNA motors of opposite polarity to drive translocation and unwinding of duplex DNA. We hypothesized that this organization may explain the exceptionally high rate and processivity of DNA
Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme
- J Biol Chem
, 1992
"... A fluorescence assay was used to measure the pro-cessivity of Escherichia coli recBCD enzyme helicase activity. Under standard conditions, recBCD enzyme unwinds an average of 30 k 3.2 kilobase pairs (kb)/ DNA end before dissociating. The average processivity (Pobs) of DNA unwinding under these condi ..."
Abstract
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Cited by 17 (6 self)
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A fluorescence assay was used to measure the pro-cessivity of Escherichia coli recBCD enzyme helicase activity. Under standard conditions, recBCD enzyme unwinds an average of 30 k 3.2 kilobase pairs (kb)/ DNA end before dissociating. The average processivity (Pobs) of DNA unwinding under
Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding
, 2004
"... We have developed and optimized a stopped-flow fluorescence assay for use in studying DNA unwinding catalyzed by Escherichia coli RecBCD helicase. This assay monitors changes in fluorescence resonance energy transfer (FRET) between a pair of fluorescent probes (Cy3 donor and Cy5 acceptor) placed on ..."
Abstract
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Cited by 16 (8 self)
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We have developed and optimized a stopped-flow fluorescence assay for use in studying DNA unwinding catalyzed by Escherichia coli RecBCD helicase. This assay monitors changes in fluorescence resonance energy transfer (FRET) between a pair of fluorescent probes (Cy3 donor and Cy5 acceptor) placed
DNA unwinding heterogeneity by RecBCD results from static molecules able to equilibrate
- Nature
, 2013
"... Single-molecule studies can overcome the complications of asynchrony and ensemble-averaging in bulk-phase measurements, provide mechanistic insights into molecular activities, and reveal interesting variations between individual molecules1–3. The application of these techniques to the RecBCD helicas ..."
Abstract
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Cited by 3 (0 self)
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helicase of Escherichia coli has resolved some long-standing discrepancies, and has provided otherwise unattainable mechanistic insights into its enzymatic behavior4–6. Enigmatically, the DNA unwinding rates of individual enzyme molecules are seen to vary significantly6–8, yet the origin
Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
- Biochemistry
, 1989
"... ABSTRACT: We describe an assay to measure the extent of enzymatic unwinding of DNA by a DNA helicase. This assay takes advantage of the quenching of the intrinsic protein fluorescence of Escherichia coli SSB protein upon binding to ssDNA and is used to characterize the DNA unwinding activity of recB ..."
Abstract
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Cited by 29 (7 self)
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enzyme. Unwinding in this assay is dependent on the presence of recBCD enzyme and linear dsDNA, is consistent with the known properties of recBCD enzyme, and closely parallels other methods for measuring recBCD enzyme helicase activity. The effects of varying temperature, substrate concentrations, enzyme
Gam protein inhibits the helicase and Chi stimulated recombination activities of Eschenchia coli RecBCD enzyme
- J
, 1991
"... The Gam protein was isolated from cells containing a Gam-producing plasmid. The purified Gam protein was found to bind to RecBCD without displacing any of its subunits. Gam was shown to inhibit all known enzymatic activities of RecBCD: ATP-dependent single- and double-stranded DNA exonucleases, ATP- ..."
Abstract
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Cited by 20 (4 self)
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in Escherichia coli proceeds through the RecBCD pathway. The RecBCD enzyme (also known as ExoV) has five known activities: ATP-dependent double-stranded and single-stranded DNA (dsDNA and ssDNA, respectively) exonu-cleases, an ATP-stimulated ssDNA endonuclease, an ATP-dependent unwinding activity, and a DNA
A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme
, 1999
"... Homologous recombination and double-stranded DNA break repair in Escherichia coli are initiated by the multifunctional RecBCD enzyme. After binding to a dou-ble-stranded DNA end, the RecBCD enzyme unwinds and degrades the DNA processively. This processing is regulated by the recombination hot spot, ..."
Abstract
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Cited by 8 (1 self)
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Homologous recombination and double-stranded DNA break repair in Escherichia coli are initiated by the multifunctional RecBCD enzyme. After binding to a dou-ble-stranded DNA end, the RecBCD enzyme unwinds and degrades the DNA processively. This processing is regulated by the recombination hot spot
Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding
- J. Mol. Biol
, 2004
"... The kinetic mechanism by which Escherichia coli RecBCD helicase unwinds duplex DNA was studied using a fluorescence stopped-flow method. Single turnover DNA unwinding experiments were performed using a series of fluorescently labeled DNA substrates containing duplex DNA regions ranging from 24 bp to ..."
Abstract
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Cited by 14 (4 self)
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The kinetic mechanism by which Escherichia coli RecBCD helicase unwinds duplex DNA was studied using a fluorescence stopped-flow method. Single turnover DNA unwinding experiments were performed using a series of fluorescently labeled DNA substrates containing duplex DNA regions ranging from 24 bp
Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli RecA and RecBCD proteins
- J. Biol. Chem
, 1989
"... We have established an in vitro reaction in which heteroduplex DNA formation is dependent on the con-certed actions of recA and recBCD proteins, the major components of the recBCD pathway of genetic recom-bination in vivo. We find that heteroduplex DNA for-mation requires three distinct enzymatic fu ..."
Abstract
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Cited by 7 (4 self)
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functions: first, the helicase activity of recBCD enzyme initiates heteroduplex DNA formation by unwinding the linear double-stranded DNA molecule to transiently form sin-gle-stranded DNA (ssDNA); second, recA protein traps this ssDNA before it reanneals; third, recA protein catalyzes the pairing of this ss
Results 1 - 10
of
163
