ArticleProceedings of the National Academy of Sciences of the United States of America2009
The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.Nucleic acids research · 2026Article
- Structures of DnaA domain I reveal a dimer conserved across Actinomycetes.Nucleic acids research · 2026Article
- Menadione reduces the expression of virulence- and colonization-associated genes inMicrobiology (Reading, England) · 2025Article
- The DNA replication initiation protein DnaD recognises a specific strand of the Bacillus subtilis chromosome origin.Nucleic acids research · 2023Article
- SirA inhibits the essential DnaA:DnaD interaction to block helicase recruitment during Bacillus subtilis sporulation.Nucleic acids research · 2023Article
- Questing functions and structures of hypothetical proteins from Campylobacter jejuni: a computer-aided approach.Bioscience reports · 2020Article
- A nucleotide-dependent oligomerization of the Escherichia coli replication initiator DnaA requires residue His136 for remodeling of the chromosomal origin.Nucleic acids research · 2020Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- Identification of a basal system for unwinding a bacterial chromosome origin.The EMBO journal · 2019Article
- DNA replication initiation in Bacillus subtilis: structural and functional characterization of the essential DnaA-DnaD interaction.Nucleic acids research · 2019Article
- NapM enhances the survival ofCommunications biology · 2019Article
- Cryptic protein interactions regulate DNA replication initiation.Molecular microbiology · 2019Article
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- Rv0004 is a new essential member of the mycobacterial DNA replication machinery.PLoS genetics · 2017Article
- Control of bacterial chromosome replication by non-coding regions outside the origin.Current genetics · 2017Review
- Review
- Review
- '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
- Tetramerization and interdomain flexibility of the replication initiation controller YabA enables simultaneous binding to multiple partners.Nucleic acids research · 2016Article
- Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids.Frontiers in molecular biosciences · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial DNA replication requires DnaA, an AAA+ ATPase that initiates replication at a specific chromosome region, oriC, and is regulated by species-specific regulators that directly bind DnaA. HobA is a DnaA binding protein, recently identified as an essential regulator of DNA replication in Helicobacter pylori. We report the crystal structure of HobA in complex with domains I and II of DnaA (DnaA(I-II)) from H. pylori, the first structure of DnaA bound to one of its regulators. Biochemical characterization of the complex formed shows that a tetramer of HobA binds four DnaA(I-II) molecules, and that DnaA(I-II) is unable to oligomerize by itself. Mutagenesis and protein-protein interaction studies demonstrate that some of the residues located at the HobA-DnaA(I-II) interface in the structure are necessary for complex formation. Introduction of selected mutations into H. pylori shows that the disruption of the interaction between HobA and DnaA is lethal for the bacteria. Remarkably, the DnaA binding site of HobA is conserved in DiaA from Escherichia coli, suggesting that the structure of the HobA/DnaA complex represents a model for DnaA regulation in other Gram-negative bacteria. Our data, together with those from other studies, indicate that HobA could play a crucial scaffolding role during the initiation of replication in H. pylori by organizing the first step of DnaA oligomerization and attachment to oriC.
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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.