The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition
about
The solution structure of the C-terminal domain of the Mu B transposition proteinA new role for translation initiation factor 2 in maintaining genome integrityRecombinational repair of DNA damage in Escherichia coli and bacteriophage lambdaStringent response processes suppress DNA damage sensitivity caused by deficiency in full-length translation initiation factor 2 or PriA helicaseThe AAA+ ClpX machine unfolds a keystone subunit to remodel the Mu transpososome.Role of PriA in replication fork reactivation in Escherichia coli.Studies on a "jumping gene machine": higher-order nucleoprotein complexes in Mu DNA transposition.PriA and phage T4 gp59: factors that promote DNA replication on forked DNA substrates microreview.Early steps of Bacillus subtilis primosome assembly.Mu insertions are repaired by the double-strand break repair pathway of Escherichia coliRescue of arrested replication forks by homologous recombinationHandoff from recombinase to replisome: insights from transpositionMultiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12.Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA.The Mu story: how a maverick phage moved the field forwardRecruitment 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.Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12.PriA mutations that affect PriA-PriC function during replication restart.Properties of the PriA helicase domain and its role in binding PriA to specific DNA structures.Mechanisms of bacterial DNA replication restart.DNA binding of PriA protein requires cooperation of the N-terminal D-loop/arrested-fork binding and C-terminal helicase domains.Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway.Host factors that promote transpososome disassembly and the PriA-PriC pathway for restart primosome assembly.
P2860
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P2860
The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@ast
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@en
type
label
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@ast
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@en
prefLabel
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@ast
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@en
P2860
P356
P1433
P1476
The phiX174-type primosome pro ...... bacteriophage Mu transposition
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/16.22.6886
P407
P577
1997-11-01T00:00:00Z