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

Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo.

The Biochemical journal - 15 Jul 2005

Soni Rajesh K, Mehra Parul, Mukhopadhyay Gauranga, Dhar Suman Kumar

Abstract excerpt

In Escherichia coli, DnaC is essential for loading DnaB helicase at oriC (the origin of chromosomal DNA replication). The question arises as to whether this model can be generalized to other species, since many eubacterial species fail to possess dnaC in their genomes. Previously, we have reported the characterization of HpDnaB (Helicobacter pylori DnaB) both in vitro and in vivo. Interestingly, H. pylori does...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to DNA Helicases
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Enzymologic

Share to Genetic Complementation Test

Share to Helicobacter pylori

Share to Substrate Specificity

Share to Two-Hybrid System Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 15836434
DOI: 10.1042/BJ20050062
PMCID: PMC1175132

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo.PMID 15836434Read ↗

Functional characterization of Helicobacter pylori DnaB helicaseSemantic proximity Read ↗

Assembly of Helicobacter pylori initiation complex is determined by sequence-specific and topology-sensitive DnaA-oriC interactions.Semantic proximity Read ↗

Isolation and characterization of temperature-sensitive mutants of the Staphylococcus aureus dnaC gene.Semantic proximity Read ↗

Putative Cooperative ATP-DnaA Binding to Double-Stranded DnaA Box and Single-Stranded DnaA-Trio Motif upon Helicobacter pylori Replication Initiation Complex Assembly.Semantic proximity Read ↗

Biochemical characterization of Escherichia coli DnaC variants that alter DnaB helicase loading onto DNA.Semantic proximity Read ↗

Helicobacter pylori single-stranded DNA binding protein--functional characterization and modulation of H. pylori DnaB helicase activity.Semantic proximity Read ↗

Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454.Semantic proximity Read ↗

Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase.Semantic proximity Read ↗

Identification of a putative chromosomal replication origin from Helicobacter pylori and its interaction with the initiator protein DnaASemantic proximity Read ↗

The atypical response regulator HP1021 controls formation of the Helicobacter pylori replication initiation complex.Semantic proximity Read ↗

Helicobacter pylori AddAB helicase‐nuclease and RecA promote recombination‐related DNA repair and survival during stomach colonizationSemantic proximity Read ↗

Substitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.Semantic proximity Read ↗

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