Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA. (Q41901200)

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scientific article published on 9 January 2007

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English	Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA.	scientific article published on 9 January 2007

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA. (English)

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Europe PubMed Central

PMC publication ID

13 October 2017

Escherichia coli

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based on heuristic

inferred from title

author name string

Stephen L Slocum

1

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Jackson A Buss

2

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Europe PubMed Central

PMC publication ID

13 October 2017

Yuji Kimura

3

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Europe PubMed Central

PMC publication ID

13 October 2017

Piero R Bianco

4

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Europe PubMed Central

PMC publication ID

13 October 2017

language of work or name

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publication date

9 January 2007

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Europe PubMed Central

PMC publication ID

13 October 2017

Journal of Molecular Biology

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Europe PubMed Central

PMC publication ID

13 October 2017

367

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Europe PubMed Central

PMC publication ID

13 October 2017

3

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

647-664

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Mechanism of translocation and kinetics of DNA unwinding by the helicase RecG.

1 reference

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Stabilization of a stalled replication fork by concerted actions of two helicases

1 reference

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PriA helicase and SSB interact physically and functionally.

1 reference

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Topological domain structure of the Escherichia coli chromosome

1 reference

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Interplay between DNA replication, recombination and repair based on the structure of RecG helicase

1 reference

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Situational repair of replication forks: roles of RecG and RecA proteins

1 reference

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Molecular views of recombination proteins and their control

1 reference

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Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: Structures and properties of isolated helicases

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A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins

1 reference

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Heparin-protein interactions

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Genome stability and the processing of damaged replication forks by RecG.

1 reference

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Structural analysis of DNA replication fork reversal by RecG

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Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled

1 reference

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Rescue of stalled replication forks by RecG: simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation

1 reference

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Topological challenges to DNA replication: conformations at the fork

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Processive translocation and DNA unwinding by individual RecBCD enzyme molecules

1 reference

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Biochemical characterization of the DNA helicase activity of the escherichia coli RecQ helicase

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Characterisation of the catalytically active form of RecG helicase

1 reference

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Translocation step size and mechanism of the RecBC DNA helicase

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Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda

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Knot what we thought before: the twisted story of replication

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Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA

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RecG helicase activity at three- and four-strand DNA structures.

1 reference

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The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation

1 reference

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The structure of supercoiled intermediates in DNA replication

1 reference

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RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination

1 reference

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Processing of recombination intermediates by the RuvABC proteins

1 reference

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DNA Binding and Helicase Domains of the Escherichia Coli Recombination Protein RecG

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The DNA replication protein PriA and the recombination protein RecG bind D-loops

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ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase

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The RecG branch migration protein of Escherichia coli dissociates R-loops.

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Surveying a supercoil domain by using the gamma delta resolution system in Salmonella typhimurium

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Dissociation of synthetic Holliday junctions by E. coli RecG protein.

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Biochemistry of homologous recombination in Escherichia coli

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The inverted repeat as a recognizable structural feature in supercoiled DNA molecules

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Identifiers

10.1016/J.JMB.2007.01.007

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

ResearchGate publication ID

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