Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork

scientific article published in August 2000

Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M001800200
P698PubMed publication ID10833513

P2093author name stringP Chang
K J Marians
P2860cites workCrystal structure of the N-terminal domain of the DnaB hexameric helicaseQ27619052
Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7Q27620078
Role of PriA in replication fork reactivation in Escherichia coliQ33805205
PriA-directed replication fork restart in Escherichia coliQ33885421
DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant rangeQ34057692
Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicasesQ34387475
DNA or RNA priming of bacteriophage G4 DNA synthesis by Escherichia coli dnaG proteinQ35035406
Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitroQ35072388
Defect in general priming conferred by linker region mutants of Escherichia coli dnaBQ35610522
Prokaryotic DNA replicationQ35671078
Isolation of an intermediate which precedes dnaG RNA polymerase participation in enzymatic replication of bacteriophage phi X174 DNAQ35987377
Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNAQ35989806
Replication fork assembly at recombination intermediates is required for bacterial growthQ36443290
Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA.Q36685433
A structural model for the Escherichia coli DnaB helicase based on electron microscopy data.Q36693128
The interaction between helicase and primase sets the replication fork clockQ38353757
The extreme C terminus of primase is required for interaction with DnaB at the replication forkQ38353761
Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movementQ38361453
Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.Q38642649
Organization and evolution of bacterial and bacteriophage primase-helicase systemsQ44080673
In vitro synthesis of bacteriophage f1 proteinsQ44124705
The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT.Q54369324
Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication.Q54580631
The ordered assembly of the phiX174-type primosome. II. Preservation of primosome composition from assembly through replication.Q54586678
The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes.Q54586682
Tau protects beta in the leading-strand polymerase complex at the replication fork.Q54593379
Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity.Q54627242
The HexamericE. coliDnaB Helicase can Exist in Different Quarternary StatesQ56937904
P433issue34
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)26187-26195
P577publication date2000-08-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleIdentification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork
P478volume275

Reverse relations

cites work (P2860)
Q39689763Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P.
Q36440552Bacteriophage replication modules
Q41433325Class-specific restrictions define primase interactions with DNA template and replicative helicase
Q36492284Coumarin-based inhibitors of Bacillus anthracis and Staphylococcus aureus replicative DNA helicase: chemical optimization, biological evaluation, and antibacterial activities
Q40458920DNA Helicases.
Q42576825DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading.
Q47603277DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase
Q58783987DnaG Primase-A Target for the Development of Novel Antibacterial Agents
Q40969310DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings
Q54540612Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin.
Q24796593Gene discovery within the planctomycete division of the domain Bacteria using sequence tags from genomic DNA libraries
Q27650607Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
Q43203582In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues
Q38349286Mechanism and Stoichiometry of Interaction of DnaG Primase with DnaB Helicase of Escherichia coli in RNA Primer Synthesis
Q27641332Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis
Q54454646Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase.
Q39109316Non-Canonical Replication Initiation: You're Fired!
Q27681112Nucleotide and Partner-Protein Control of Bacterial Replicative Helicase Structure and Function
Q24651057Primase directs the release of DnaC from DnaB
Q28357054Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile
Q33999043Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions
Q41343446Replication Initiation in Bacteria
Q33940331Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex
Q38601246Replisome Dynamics during Chromosome Duplication
Q33698530Replisome mechanics: lagging strand events that influence speed and processivity
Q39687119Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus
Q27648844Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
Q34584666The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel.
Q52656083The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.
Q36895278The bacterial DnaC helicase loader is a DnaB ring breaker
Q36153494The bacterial helicase-primase interaction: a common structural/functional module.