A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.
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Structure of the N-Terminal Oligomerization Domain of DnaD Reveals a Unique Tetramerization Motif and Provides Insights into Scaffold FormationThe crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNAA novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loaderStructure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assemblyPrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileViral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replicationDiscovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid.The cyanobacterial cell division factor Ftn6 contains an N-terminal DnaD-like domainDnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.Mutations altering the interplay between GkDnaC helicase and DNA reveal an insight into helicase unwinding'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.The Bacillus subtilis DnaD protein: a putative link between DNA remodeling and initiation of DNA replication.The DNA-remodelling activity of DnaD is the sum of oligomerization and DNA-binding activities on separate domainsHelicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.Characterization of Staphylococcus aureus Primosomal DnaD Protein: Highly Conserved C-Terminal Region Is Crucial for ssDNA and PriA Helicase Binding but Not for DnaA Protein-Binding and Self-TetramerizationThe bacterial DnaC helicase loader is a DnaB ring breaker.Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.Loading mechanisms of ring helicases at replication origins.Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.Functional characterization of Helicobacter pylori DnaB helicase.DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings.Inhibition of Staphylococcus aureus PriA Helicase by Flavonol Kaempferol.Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis.The primosomal protein DnaD inhibits cooperative DNA binding by the replication initiator DnaA in Bacillus subtilis.The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication.Bacillus subtilis RarA modulates replication restart
P2860
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P2860
A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@en
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@nl
type
label
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@en
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@nl
prefLabel
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@en
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@nl
P2860
P356
P1476
A functional interaction betwe ...... DNA helicase DnaB in Bacillus.
@en
P2860
P304
P356
10.1093/NAR/30.4.966
P407
P577
2002-02-01T00:00:00Z