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A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme

by Daniel G. Anderson, Jason J. Churchill, Stephen C. Kowalczykowski , 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 - Cited by 8 (1 self) - Add to MetaCart
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

RecBCD enzyme and the repair of double-stranded DNA breaks

by Mark S. Dillingham, Stephen C. Kowalczykowski, Mark S. Dillingham, Stephen C. Kowalczykowski - Microbiol. Mol. Rev , 2008
"... Updated information and services can be found at: ..."
Abstract - Cited by 29 (4 self) - Add to MetaCart
Updated information and services can be found at:

Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme

by Deana A. Arnold, Stephen C. Kowalczykowski‡¶i - J Biol Chem , 2000
"... Although the RecB2109CD enzyme retains most of the biochemical functions associated with the wild-type RecBCD enzyme, it is completely defective for genetic recombination. Here, we demonstrate that the mutant enzyme exhibits an aberrant double-stranded DNA exo-nuclease activity, intrinsically produc ..."
Abstract - Cited by 20 (1 self) - Add to MetaCart
Although the RecB2109CD enzyme retains most of the biochemical functions associated with the wild-type RecBCD enzyme, it is completely defective for genetic recombination. Here, we demonstrate that the mutant enzyme exhibits an aberrant double-stranded DNA exo-nuclease activity, intrinsically

Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme

by Linda J. Roman, Angela K. Egglestonp, Stephen C. Kowalczykowskiq - 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 - Cited by 17 (6 self) - Add to MetaCart
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

RecBCD Enzyme: Relationship of ATP Hydrolysis to the Unwinding of Duplex DNA+

by B. Cold Spring, S. C. Biochemistry, Linda J. Roman, Stephen C. Kowalczykowski , 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

The Translocating RecBCD Enzyme Stimulates Recombination by Directing RecA Protein

by unknown authors
"... onto ssDNA in a x-Regulated Manner ..."
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onto ssDNA in a x-Regulated Manner

Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay

by Linda J. Roman, Stephen C. Kowalczykowski - 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 - Cited by 29 (7 self) - Add to MetaCart
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

by Kenan C. Murphy - 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 - Cited by 20 (4 self) - Add to MetaCart
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

The DNA replication fork blocked at the Ter site may be an entrance for the RecBCD enzyme into duplex

by T Horiuchi, Y Fujimura, H Nishitani, T Kobayashi, M Hidaka, Takashi Horiuchi, L Yohko Fujimura, T Hideo Nishitani , 1994
"... into duplex DNA. may be an entrance for the RecBCD enzyme The DNA replication fork blocked at the Ter site ..."
Abstract - Cited by 9 (2 self) - Add to MetaCart
into duplex DNA. may be an entrance for the RecBCD enzyme The DNA replication fork blocked at the Ter site

Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme

by Mark S. Dillingham, Martin R. Webb, Stephen C. Kowalczykowski - 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 - Cited by 11 (3 self) - Add to MetaCart
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
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