ArticleOpen biology2016
Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Analysis of essential genes inJournal of bacteriology · 2025Article
- Characterization of DnaB-DnaG Interaction in M. tuberculosis Using Small-Angle X-ray Scattering-Based Dissociation Assay.Chembiochem : a European journal of chemical biology · 2025Article
- Analysis of Essential Genes inbioRxiv : the preprint server for biology · 2025Article
- Primase promotes the competition between transcription and replication on the same template strand resulting in DNA damage.Nature communications · 2024Article
- Inhibition of Replication Fork Formation and Progression: Targeting the Replication Initiation and Primosomal Proteins.International journal of molecular sciences · 2023Review
- Theoretical Development of DnaG Primase as a Novel Narrow-Spectrum Antibiotic Target.ACS omega · 2022Article
- Inferring primase-DNA specific recognition using a data driven approach.Nucleic acids research · 2021Article
- The Alarmone (p)ppGpp Regulates Primer Extension by Bacterial Primase.Journal of molecular biology · 2021Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- Genome Location Dictates the Transcriptional Response to PolC Inhibition inAntimicrobial agents and chemotherapy · 2019Article
- Plant organellar DNA primase-helicase synthesizes RNA primers for organellar DNA polymerases using a unique recognition sequence.Nucleic acids research · 2017Article
- DNA replication proteins as potential targets for antimicrobials in drug-resistant bacterial pathogens.The Journal of antimicrobial chemotherapy · 2017Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
DNA replication is an essential and conserved process in all domains of life and may serve as a target for the development of new antimicrobials. However, such developments are hindered by subtle mechanistic differences and limited understanding of DNA replication in pathogenic microorganisms. Clostridium difficile is the main cause of healthcare-associated diarrhoea and its DNA replication machinery is virtually uncharacterized. We identify and characterize the mechanistic details of the putative replicative helicase (CD3657), helicase-loader ATPase (CD3654) and primase (CD1454) of C. difficile, and reconstitute helicase and primase activities in vitro We demonstrate a direct and ATP-dependent interaction between the helicase loader and the helicase. Furthermore, we find that helicase activity is dependent on the presence of primase in vitro The inherent trinucleotide specificity of primase is determined by a single lysine residue and is similar to the primase of the extreme thermophile Aquifex aeolicus. However, the presence of helicase allows more efficient de novo synthesis of RNA primers from non-preferred trinucleotides. Thus, loader-helicase-primase interactions, which crucially mediate helicase loading and activation during DNA replication in all organisms, differ critically in C. difficile from that of the well-studied Gram-positive Bacillus subtilis model.
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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.