The Escherichia coli replisome is inherently DNA damage tolerant
about
PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replicationPrimPol, an archaic primase/polymerase operating in human cellsRescuing stalled or damaged replication forksNew insights into replisome fluidity during chromosome replicationRegulation of Mutagenic DNA Polymerase V Activation in Space and TimeReplication stress: getting back on trackA Genetic Selection for dinB Mutants Reveals an Interaction between DNA Polymerase IV and the Replicative Polymerase That Is Required for Translesion SynthesisDNA flap creation by the RarA/MgsA protein of Escherichia coliStringent response processes suppress DNA damage sensitivity caused by deficiency in full-length translation initiation factor 2 or PriA helicaseRegression of replication forks stalled by leading-strand template damage: I. Both RecG and RuvAB catalyze regression, but RuvC cleaves the holliday junctions formed by RecG preferentially.Regression of replication forks stalled by leading-strand template damage: II. Regression by RecA is inhibited by SSBRecombination and replication.Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.Replisome-mediated translesion synthesis and leading strand template lesion skipping are competing bypass mechanismsBacterial Proliferation: Keep Dividing and Don't Mind the Gap.The progression of replication forks at natural replication barriers in live bacteriaSingle-Molecule Observation of DNA Replication Repair Pathways in E. coli.Cellular characterization of the primosome and rep helicase in processing and restoration of replication following arrest by UV-induced DNA damage in Escherichia coli.Low doses of ultraviolet radiation and oxidative damage induce dramatic accumulation of mitochondrial DNA replication intermediates, fork regression, and replication initiation shiftT7 replisome directly overcomes DNA damage.Protein-DNA complexes are the primary sources of replication fork pausing in Escherichia coliMutations for Worse or Better: Low-Fidelity DNA Synthesis by SOS DNA Polymerase V Is a Tightly Regulated Double-Edged SwordPolymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.DNA damage responses in prokaryotes: regulating gene expression, modulating growth patterns, and manipulating replication forks.Low-molecular-weight DNA replication intermediates in Escherichia coli: mechanism of formation and strand specificity.Early days of DNA repair: discovery of nucleotide excision repair and homology-dependent recombinational repair.Direct observation of stalled fork restart via fork regression in the T4 replication system.The DNA translocase FANCM/MHF promotes replication traverse of DNA interstrand crosslinks.Multiple strategies for translesion synthesis in bacteriaMechanisms of mutagenesis: DNA replication in the presence of DNA damage.Mechanisms of Post-Replication DNA RepairThe Intra-S Checkpoint Responses to DNA Damage.Chronology in lesion tolerance gives priority to genetic variability.A proposal: Source of single strand DNA that elicits the SOS response.Impediments to replication fork movement: stabilisation, reactivation and genome instability.Replication-fork dynamics.Discontinuous leading-strand synthesis: a stop-start story.Homologous recombination as a replication fork escort: fork-protection and recovery.A Replisome's journey through the bacterial chromosome.Repriming by PrimPol is critical for DNA replication restart downstream of lesions and chain-terminating nucleosides.
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The Escherichia coli replisome is inherently DNA damage tolerant
description
2011 nî lūn-bûn
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2011年の論文
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2011年論文
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2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
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2011年论文
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2011年论文
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2011年论文
@zh-cn
name
The Escherichia coli replisome is inherently DNA damage tolerant
@en
type
label
The Escherichia coli replisome is inherently DNA damage tolerant
@en
prefLabel
The Escherichia coli replisome is inherently DNA damage tolerant
@en
P2860
P356
P1433
P1476
The Escherichia coli replisome is inherently DNA damage tolerant
@en
P2093
Joseph T P Yeeles
Kenneth J Marians
P2860
P304
P356
10.1126/SCIENCE.1209111
P407
P577
2011-10-01T00:00:00Z