ArticleThe Biochemical journal2005
Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021Review
- Blocking the Trigger: Inhibition of the Initiation of Bacterial Chromosome Replication as an Antimicrobial Strategy.Antibiotics (Basel, Switzerland) · 2019Review
- Structural insight into β-Clamp and its interaction with DNA Ligase in Helicobacter pylori.Scientific reports · 2016Article
- 'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.Nucleic acids research · 2016Article
- Structure and primase-mediated activation of a bacterial dodecameric replicative helicase.Nucleic acids research · 2015Article
- A Replisome's journey through the bacterial chromosome.Frontiers in microbiology · 2015Review
- Intracellular locations of replication proteins and the origin of replication during chromosome duplication in the slowly growing human pathogen Helicobacter pylori.Journal of bacteriology · 2014Article
- Crystal structure and mode of helicase binding of the C-terminal domain of primase from Helicobacter pylori.Journal of bacteriology · 2013Article
- Loading mechanisms of ring helicases at replication origins.Molecular microbiology · 2012Review
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter spp.Microbiology and molecular biology reviews : MMBR · 2010Review
- The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori.PloS one · 2009Article
- The domain structure of Helicobacter pylori DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function.Nucleic acids research · 2007Article
- Replication Initiation in Bacteria.The EnzymesReview
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 not have a DnaC homologue. Using two different E. coli dnaC (EcdnaC) temperature-sensitive mutant strains, we report here the complementation of EcDnaC function by HpDnaB in vivo. These observations strongly suggest that HpDnaB can bypass EcDnaC activity in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.