Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
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The RuvABC resolvasomeA YY1-INO80 complex regulates genomic stability through homologous recombination-based repairWRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication forkHolliday junction binding activity of the human Rad51B proteinBiochemistry of homologous recombination in Escherichia coliThe Bloom's syndrome gene product promotes branch migration of holliday junctionsMicrobial antigenic variation mediated by homologous DNA recombinationCrystal structure of the Holliday junction DNA in complex with a single RuvA tetramerThe INO80 ATP-dependent chromatin remodeling complex is a nucleosome spacing factorRecombinational repair of DNA damage in Escherichia coli and bacteriophage lambdaCentral role of the Holliday junction helicase RuvAB in vlsE recombination and infectivity of Borrelia burgdorferi.Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest.ruvA Mutants that resolve Holliday junctions but do not reverse replication forksHolliday junction-binding peptides inhibit distinct junction-processing enzymesATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicaseThe RuvC protein dimer resolves Holliday junctions by a dual incision mechanism that involves base-specific contactsFunctional interactions between the holliday junction resolvase and the branch migration motor of Escherichia coli.Recombinational repair and restart of damaged replication forks.The RuvA homologues from Mycoplasma genitalium and Mycoplasma pneumoniae exhibit unique functional characteristics.Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: a versatile couple with roles in replication and recombination.Biochemical analysis of the DNA unwinding and strand annealing activities catalyzed by human RECQ1.RuvAB and RecG are not essential for the recovery of DNA synthesis following UV-induced DNA damage in Escherichia coliRecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination.Assembly of the Escherichia coli RuvABC resolvasome directs the orientation of holliday junction resolution.Cloning, sequencing, and expression of ruvB and characterization of RuvB proteins from two distantly related thermophilic eubacteria.The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA.Dissociation of RecA filaments from duplex DNA by the RuvA and RuvB DNA repair proteinsRuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro.Unique and important consequences of RECQ1 deficiency in mammalian cells.RecG interacts directly with SSB: implications for stalled replication fork regression.Functions of the gene products of Escherichia coli.Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repairDirect observation of RuvAB-catalyzed branch migration of single Holliday junctions.Single-molecule study of RuvAB-mediated Holliday-junction migration.Control of helicase loading in the coupled DNA replication and recombination systems of bacteriophage T4.The E.coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB.Rad54, the motor of homologous recombination.Rvb1-Rvb2: essential ATP-dependent helicases for critical complexes.Characterization of the operon encoding the Holliday junction helicase RuvAB from Mycoplasma genitalium and its role in mgpB and mgpC gene variation.Holliday junction resolvases.
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Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on June 1992
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
@en
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
@nl
type
label
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
@en
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
@nl
prefLabel
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
@en
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions.
@nl
P2093
P2860
P356
P1476
Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.12.5452
P407
P577
1992-06-01T00:00:00Z