ArticleNucleic acids research2017
Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- The loop domains of the E. coli β sliding clamp are required for Hda-dependent inactivation of DnaA.Genetics · 2026Article
- The iron-sulfur accelerator YgfZ modulates genome-wide IHF-binding dynamics to regulate replication initiation inFrontiers in microbiology · 2026Article
- Responses to Ligand Binding in the Bacterial DNA Sliding Clamp "β-Clamp" Manifest in Dynamic Allosteric Effects.Proteins · 2025Article
- Negative DNA supercoiling enhances DARS2 binding of DNA-bending protein IHF in the activation of Fis-dependent ATP-DnaA production.Nucleic acids research · 2025Article
- Exquisite selectivity of griselimycin extends to beta subunit of DNA polymerases from Gram-negative bacterial pathogens.Communications biology · 2024Article
- The bacterial DNA sliding clamp, β-clamp: structure, interactions, dynamics and drug discovery.Cellular and molecular life sciences : CMLS · 2024Review
- IHF and Fis asInternational journal of molecular sciences · 2023Review
- Review
- Negative feedback for DARS2-Fis complex by ATP-DnaA supports the cell cycle-coordinated regulation for chromosome replication.Nucleic acids research · 2021Article
- Elevated Levels of the Escherichia coliJournal of bacteriology · 2021Article
- Cell Size Is Coordinated with Cell Cycle by Regulating Initiator Protein DnaA in E. coli.Biophysical journal · 2020Article
- Mechanisms of Theta Plasmid Replication in Enterobacteria and Implications for Adaptation to Its Host.EcoSal Plus · 2020Review
- HdaB: a novel and conserved DnaA-related protein that targets the RIDA process to stimulate replication initiation.Nucleic acids research · 2020Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- DNA replication initiation in Bacillus subtilis: structural and functional characterization of the essential DnaA-DnaD interaction.Nucleic acids research · 2019Article
- A structural view of the initiators for chromosome replication.Current opinion in structural biology · 2018Review
- Targeting the Bacterial Orisome in the Search for New Antibiotics.Frontiers in microbiology · 2017Article
- The DnaA Cycle inFrontiers in microbiology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Regulatory inactivation of DnaA (RIDA) is one of the major regulatory mechanisms of prokaryotic replication licensing. In RIDA, the Hda-sliding clamp complex loaded onto DNA directly interacts with adenosine triphosphate (ATP)-bound DnaA and stimulates the hydrolysis of ATP to inactivate DnaA. A prediction is that the activity of Hda is tightly controlled to ensure that replication initiation occurs only once per cell cycle. Here, we determined the crystal structure of the Hda-β clamp complex. This complex contains two pairs of Hda dimers sandwiched between two β clamp rings to form an octamer that is stabilized by three discrete interfaces. Two separate surfaces of Hda make contact with the β clamp, which is essential for Hda function in RIDA. The third interface between Hda monomers occludes the active site arginine finger, blocking its access to DnaA. Taken together, our structural and mutational analyses of the Hda-β clamp complex indicate that the interaction of the β clamp with Hda controls the ability of Hda to interact with DnaA. In the octameric Hda-β clamp complex, the inability of Hda to interact with DnaA is a novel mechanism that may regulate Hda function.
Indexed as
Identifiers
What OpenQuestion holds
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.