ArticleNucleic acids research2007
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.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Integrated In Silico Analysis Reveals ABC Transporter ATP-Binding Protein as a Therapeutic Target inACS omega · 2026Article
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- Functional assignment to hypothetical proteins inBioinformation · 2022Article
- Adaptive Evolution of Lactococcus Lactis to Thermal and Oxidative Stress Increases Biomass and Nisin Production.Applied biochemistry and biotechnology · 2021Article
- '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
- Article
- Genomics Analysis of Replicative Helicase DnaB Sequences in Proteobacteria.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2014Article
- 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
- 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
- A unique 45-amino-acid region in the toprim domain of Plasmodium falciparum gyrase B is essential for its activity.Eukaryotic cell · 2009Article
- Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori.PloS one · 2009Article
- The mycobacteriophage D29 gene 65 encodes an early-expressed protein that functions as a structure-specific nuclease.Journal of bacteriology · 2009Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hexameric DnaB type replicative helicases are essential for DNA strand unwinding along with the direction of replication fork movement. These helicases in general contain an amino terminal domain and a carboxy terminal domain separated by a linker region. Due to the lack of crystal structure of a full-length DnaB like helicase, the domain structure and function of these types of helicases are not clear. We have reported recently that Helicobacter pylori DnaB helicase is a replicative helicase in vitro and it can bypass Escherichia coli DnaC activity in vivo. Using biochemical, biophysical and genetic complementation assays, here we show that though the N-terminal region of HpDnaB is required for conformational changes between C6 and C3 rotational symmetry, it is not essential for in vitro helicase activity and in vivo function of the protein. Instead, an extreme carboxy terminal region and an adjacent unique 34 amino acid insertion region were found to be essential for HpDnaB activity suggesting that these regions are important for proper folding and oligomerization of this protein. These results confer great potential in understanding the domain structures of DnaB type helicases and their related function.
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