ArticleThe Journal of biological chemistry2009
Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- A phosphorylation signal activates genome-wide transcriptional control by BfmR, the global regulator of Acinetobacter resistance and virulence.Nucleic acids research · 2025Article
- A phosphorylation signal activates genome-wide transcriptional control by BfmR, the global regulator ofbioRxiv : the preprint server for biology · 2024Article
- Molecular insights into the fine-tuning of pH-dependent ArsR-mediated regulation of the SabA adhesin in Helicobacter pylori.Nucleic acids research · 2024Article
- Antibiotic-induced ROS-mediated Fur allosterism contributes toAntimicrobial agents and chemotherapy · 2024Article
- Bifunctional protein ArsRBMC microbiology · 2023Article
- Two-component regulatory systems inFrontiers in cellular and infection microbiology · 2022Review
- Delineation of the pH-Responsive Regulon Controlled by the Helicobacter pylori ArsRS Two-Component System.Infection and immunity · 2021Article
- High-Salt Conditions Alter Transcription of Helicobacter pylori Genes Encoding Outer Membrane Proteins.Infection and immunity · 2018Article
- Crosstalk between the HpArsRS two-component system and HpNikR is necessary for maximal activation of urease transcription.Frontiers in microbiology · 2015Article
- Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.PloS one · 2014Article
- NMR study on small proteins from Helicobacter pylori for antibiotic target discovery: a review.Molecules (Basel, Switzerland) · 2013Review
- Analysis of protein expression regulated by the Helicobacter pylori ArsRS two-component signal transduction system.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Helicobacter pylori ArsS-ArsR two-component signal transduction system, comprised of a sensor histidine kinase (ArsS) and a response regulator (ArsR), allows the bacteria to regulate gene expression in response to acidic pH. We expressed and purified the full-length ArsR protein and the DNA-binding domain of ArsR (ArsR-DBD), and we analyzed the tertiary structure of the ArsR-DBD using solution nuclear magnetic resonance (NMR) methods. Both the full-length ArsR and the ArsR-DBD behaved as monomers in size exclusion chromatography experiments. The structure of ArsR-DBD consists of an N-terminal four-stranded beta-sheet, a helical core, and a C-terminal beta-hairpin. The overall tertiary fold of the ArsR-DBD is most closely related to DBD structures of the OmpR/PhoB subfamily of bacterial response regulators. However, the orientation of the N-terminal beta-sheet with respect to the rest of the DNA-binding domain is substantially different in ArsR compared with the orientation in related response regulators. Molecular modeling of an ArsR-DBD-DNA complex permits identification of protein elements that are predicted to bind target DNA sequences and thereby regulate gene transcription in H. pylori.
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Registered trials
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