about
On the viability of Escherichia coli cells lacking DNA topoisomerase IInterplay between DNA replication, recombination and repair based on the structure of RecG helicase.Avoiding and resolving conflicts between DNA replication and transcription.Protein-DNA complexes are the primary sources of replication fork pausing in Escherichia coliIs RecG a general guardian of the bacterial genome?Rep provides a second motor at the replisome to promote duplication of protein-bound DNA.Inhibiting translation elongation can aid genome duplication in Escherichia coli.The Balance between Recombination Enzymes and Accessory Replicative Helicases in Facilitating Genome Duplication.Cellular location and activity of Escherichia coli RecG proteins shed light on the function of its structurally unresolved C-terminus.DNA binding by the meningococcal RdgC protein, associated with pilin antigenic variation.Promoting and avoiding recombination: contrasting activities of the Escherichia coli RuvABC Holliday junction resolvase and RecG DNA translocase.The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA.Rep and PriA helicase activities prevent RecA from provoking unnecessary recombination during replication fork repair.Pathological replication in cells lacking RecG DNA translocase.Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase.Replication fork stalling and cell cycle arrest in UV-irradiated Escherichia coli.Avoiding chromosome pathology when replication forks collide.RecG protein and single-strand DNA exonucleases avoid cell lethality associated with PriA helicase activity in Escherichia coli.Localization of an accessory helicase at the replisome is critical in sustaining efficient genome duplicationReplication fork collisions cause pathological chromosomal amplification in cells lacking RecG DNA translocaseA soluble RecN homologue provides means for biochemical and genetic analysis of DNA double-strand break repair in Escherichia coli.RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions.RecG helicase promotes DNA double-strand break repair.DNA double strand break repair and crossing over mediated by RuvABC resolvase and RecG translocase.Maintaining replication fork integrity in UV-irradiated Escherichia coli cells.RecN protein and transcription factor DksA combine to promote faithful recombinational repair of DNA double-strand breaks.Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae.DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity.Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities.
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description
geneticist
@en
researcher (ORCID = 0000-0002-1575-3684)
@en-gb
wetenschapper
@nl
name
Robert G Lloyd
@cy
Robert G Lloyd
@en-gb
Robert G. Lloyd
@en
Robert G. Lloyd
@es
Robert G. Lloyd
@nl
type
label
Robert G Lloyd
@cy
Robert G Lloyd
@en-gb
Robert G. Lloyd
@en
Robert G. Lloyd
@es
Robert G. Lloyd
@nl
prefLabel
Robert G Lloyd
@cy
Robert G Lloyd
@en-gb
Robert G. Lloyd
@en
Robert G. Lloyd
@es
Robert G. Lloyd
@nl
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P106
P21
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0000-0002-1575-3684