Escherichia coli PriA helicase: fork binding orients the helicase to unwind the lagging strand side of arrested replication forks.
about
Structural mechanisms of PriA-mediated DNA replication restartA bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicaseThe Escherichia coli PriA helicase specifically recognizes gapped DNA substrates: effect of the two nucleotide-binding sites of the enzyme on the recognition process.Recombinational repair and restart of damaged replication forks.The Escherichia coli PriA helicase-double-stranded DNA complex: location of the strong DNA-binding subsite on the helicase domain of the protein and the affinity control by the two nucleotide-binding sites of the enzyme.Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.An aromatic-rich loop couples DNA binding and ATP hydrolysis in the PriA DNA helicase.Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.Stabilization of a stalled replication fork by concerted actions of two helicases.PriB stimulates PriA helicase via an interaction with single-stranded DNA.Survival of Helicobacter pylori in gastric acidic territory.Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA.Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexesPriA helicase and SSB interact physically and functionally.Anticipating chromosomal replication fork arrest: SSB targets repair DNA helicases to active forks.A priA Mutant Expressed in Two Pieces Has Almost Full Activity in Escherichia coli K-12.Properties of the PriA helicase domain and its role in binding PriA to specific DNA structures.Mechanisms of bacterial DNA replication restart.ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication.Escherichia coli PriA protein, two modes of DNA binding and activation of ATP hydrolysis.The DinG protein from Escherichia coli is a structure-specific helicase.Host factors that promote transpososome disassembly and the PriA-PriC pathway for restart primosome assembly.Primosome assembly requirement for replication restart in the Escherichia coli holDG10 replication mutant.Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase
P2860
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P2860
Escherichia coli PriA helicase: fork binding orients the helicase to unwind the lagging strand side of arrested replication forks.
description
2001 nî lūn-bûn
@nan
2001年の論文
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2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
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2001年論文
@zh-tw
2001年论文
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2001年论文
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2001年论文
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name
Escherichia coli PriA helicase ...... of arrested replication forks.
@en
type
label
Escherichia coli PriA helicase ...... of arrested replication forks.
@en
prefLabel
Escherichia coli PriA helicase ...... of arrested replication forks.
@en
P356
P1476
Escherichia coli PriA helicase ...... of arrested replication forks.
@en
P2093
P304
P356
10.1006/JMBI.2001.4930
P407
P577
2001-10-01T00:00:00Z