Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis.

The Journal of biological chemistry - 26 Dec 2003

Mitkova Atanaska V, Khopde Sujata M, Biswas Subhasis B

Abstract excerpt

Initiation and synthesis of RNA primers in the lagging strand of the replication fork in Escherichia coli requires the replicative DnaB helicase and the DNA primase, the DnaG gene product. In addition, the physical interaction between these two replication enzymes appears to play a role in the initiation of chromosomal DNA replication. In vitro, DnaB helicase stimulates primase to synthesize primers on...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anisotropy
Share to Chromatography, Gel
Share to Chromatography, High Pressure Liquid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to DNA Primase

Share to DNA, Single-Stranded

Share to Fluorescent Dyes

Share to Oligonucleotides

Source

Identifiers

PMID: 14557266
DOI: 10.1074/jbc.M308956200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis.PMID 14557266Read ↗

DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings.Semantic proximity Read ↗

Purification and characterization of a mutant DnaB protein specifically defective in ATP hydrolysis.Semantic proximity Read ↗

In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues.Semantic proximity Read ↗

Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA.Semantic proximity Read ↗

A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli.Semantic proximity Read ↗

Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system.Semantic proximity Read ↗

Defect in general priming conferred by linker region mutants of Escherichia coli dnaB.Semantic proximity Read ↗

Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin.Semantic proximity Read ↗

Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.Semantic proximity Read ↗

Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli.Semantic proximity Read ↗

Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus.Semantic proximity Read ↗

Incoming nucleotide binds to Klenow ternary complex leading to stable physical sequestration of preceding dNTP on DNA.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.