Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. (Q47792009)

5 February 2018

title

Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. (English)

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1

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author name string

Lloyd RG

series ordinal

2

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language of work or name

English

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publication date

1 July 1998

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Journal of Biological Chemistry

published in

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volume

273

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page(s)

19729-19739

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issue

31

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Enzymes and molecular mechanisms of genetic recombination

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The kinetics of spontaneous DNA branch migration

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The RuvABC proteins and Holliday junction processing in Escherichia coli

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Structure of a multisubunit complex that promotes DNA branch migration.

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Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction

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Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12.

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Reverse branch migration of Holliday junctions by RecG protein: a new mechanism for resolution of intermediates in recombination and DNA repair.

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A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions

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DNA binding and helicase domains of the Escherichia coli recombination protein RecG.

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

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Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli

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Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12.

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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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Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions

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Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.

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Specific recognition of cruciform DNA by nuclear protein HMG1.

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Specificity of binding to four-way junctions in DNA by bacteriophage T7 endonuclease I.

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Structural analysis of the RuvC-Holliday junction complex reveals an unfolded junction.

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The resolving enzyme CCE1 of yeast opens the structure of the four-way DNA junction

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Crossover isomer bias is the primary sequence-dependent property of immobilized Holliday junctions

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DNA sequence determinants of CAP-induced bending and protein binding affinity.

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Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion.

21 January 2018

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[20] Nuclease activity of 1,10-phenanthroline-copper in study of protein—DNA interactions

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Fluorescence energy transfer shows that the four-way DNA junction is a right-handed cross of antiparallel molecules

21 January 2018

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Crossed-stranded DNA structures for investigating the molecular dynamics of the Holliday junction

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Thermodynamic and kinetic parameters of ion condensation to polynucleotides. Outer sphere complex formed by Mg++ions

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The Structure-selectivity and Sequence-preference of the Junction-resolving Enzyme CCE1 ofSaccharomyces cerevisiae

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A new Holliday junction resolving enzyme from Schizosaccharomyces pombe that is homologous to CCE1 from Saccharomyces cerevisiae

21 January 2018

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T4 endonuclease VII. Importance of a histidine-aspartate cluster within the zinc-binding domain

21 January 2018

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The junction-resolving enzyme T7 endonuclease I: quaternary structure and interaction with DNA

21 January 2018

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Protein HU binds specifically to kinked DNA

21 January 2018

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Site-specific interaction of intercalating drugs with a branched DNA molecule

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.273.31.19729

Drug binding by branched DNA: selective interaction of the dye stains-all with an immobile junction

21 January 2018

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Model for the interaction of DNA junctions and resolving enzymes

21 January 2018

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T4 endonuclease VII selects and alters the structure of the four-way DNA junction; binding of a resolution-defective mutant enzyme

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.31.19729

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5 February 2018

PubMed ID

9677403

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5 February 2018