ArticleNucleic acids research2003
Functional characterization of Helicobacter pylori DnaB helicase.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021Review
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter.Molecules (Basel, Switzerland) · 2020Review
- The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase.Nature communications · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
- Staphylococcal SCCmec elements encode an active MCM-like helicase and thus may be replicative.Nature structural & molecular biology · 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
- Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids.Frontiers in molecular biosciences · 2016Review
- Structure and primase-mediated activation of a bacterial dodecameric replicative helicase.Nucleic acids research · 2015Article
- Loading strategies of ring-shaped nucleic acid translocases and helicases.Current opinion in structural biology · 2014Review
- 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
- Mechanisms for initiating cellular DNA replication.Annual review of biochemistry · 2013Review
- Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori.PloS one · 2009Article
- A pathogenicity island replicon in Staphylococcus aureus replicates as an unstable plasmid.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- 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
- Identification of the Mycobacterium tuberculosis SUF machinery as the exclusive mycobacterial system of [Fe-S] cluster assembly: evidence for its implication in the pathogen's survival.Journal of bacteriology · 2005Article
- Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo.The Biochemical journal · 2005Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicobacter pylori causes gastric ulcer diseases and gastric adenocarcinoma in humans. Not much is known regarding DNA replication in H.pylori that is important for cell survival. Here we report the cloning, expression and characterization of H.pylori DnaB (HpDnaB) helicase both in vitro and in vivo. Among the DnaB homologs, only Escherichia coli DnaB has been studied extensively. HpDnaB showed strong 5' to 3' helicase and ATPase activity. Interestingly, H.pylori does not have an obvious DnaC homolog which is essential for DnaB loading on the E.coli chromosomal DNA replication origin (oriC). However, HpDnaB can functionally complement the E.coli DnaB temperature-sensitive mutant at the non-permissive temperature, confirming that HpDnaB is a true replicative helicase. Escherichia coli DnaC co-eluted in the same fraction with HpDnaB following gel filtration analysis suggesting that these proteins might physically interact with each other. It is possible that a functional DnaC homolog is present in H.pylori. The complete characterization of H.pylori DnaB helicase will also help the comparative analysis of DnaB helicases among bacteria.
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