The interaction between helicase and primase sets the replication fork clock.
about
Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hostsPrimase directs the release of DnaC from DnaBStructural Mechanisms of Hexameric Helicase Loading, Assembly, and UnwindingCoordinated DNA Replication by the Bacteriophage T4 ReplisomeBinding Mechanism of Metal⋅NTP Substrates and Stringent-Response Alarmones to Bacterial DnaG-Type PrimasesNucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and FunctionStructural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.Replisome mechanics: lagging strand events that influence speed and processivityCoordinating DNA polymerase traffic during high and low fidelity synthesis.Two distantly homologous DnaG primases from Thermoanaerobacter tengcongensis exhibit distinct initiation specificities and priming activitiesTiming, coordination, and rhythm: acrobatics at the DNA replication fork.Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactionsResponse of the bacteriophage T4 replisome to noncoding lesions and regression of a stalled replication fork.Replication initiation at the Escherichia coli chromosomal originDNA primase acts as a molecular brake in DNA replication.Domain swapping reveals that the C- and N-terminal domains of DnaG and DnaB, respectively, are functional homologues.E. coli DNA replication in the absence of free β clamps.Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assemblyThe bacterial helicase-primase interaction: a common structural/functional module.DnaC traps DnaB as an open ring and remodels the domain that binds primase.Manipulating replisome dynamics to enhance lambda Red-mediated multiplex genome engineering.Single-molecule studies of complex systems: the replisome.RecA acts as a switch to regulate polymerase occupancy in a moving replication fork.Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesisMultiple C-terminal tails within a single E. coli SSB homotetramer coordinate DNA replication and repair.An in trans interaction at the interface of the helicase and primase domains of the hexameric gene 4 protein of bacteriophage T7 modulates their activities.Cycling of the E. coli lagging strand polymerase is triggered exclusively by the availability of a new primer at the replication forkHelicobacter pylori chromosomal DNA replication: current status and future perspectives.Replication-fork dynamics.Two distinct triggers for cycling of the lagging strand polymerase at the replication fork.Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.Formation of a DNA loop at the replication fork generated by bacteriophage T7 replication proteins.The DNA binding properties of the Escherichia coli RecQ helicase.The extreme C terminus of primase is required for interaction with DnaB at the replication fork.Replisome Dynamics during Chromosome Duplication.Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.RNA primer-primase complexes serve as the signal for polymerase recycling and Okazaki fragment initiation in T4 phage DNA replication.Chaperoning of a replicative polymerase onto a newly assembled DNA-bound sliding clamp by the clamp loader.Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein.
P2860
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P2860
The interaction between helicase and primase sets the replication fork clock.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
The interaction between helicase and primase sets the replication fork clock.
@en
type
label
The interaction between helicase and primase sets the replication fork clock.
@en
prefLabel
The interaction between helicase and primase sets the replication fork clock.
@en
P2860
P356
P1476
The interaction between helicase and primase sets the replication fork clock.
@en
P2093
P2860
P304
21398-21405
P356
10.1074/JBC.271.35.21398
P407
P577
1996-08-01T00:00:00Z