ArticleScientific reports2017
Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- A single helicase-binding domain of DnaG couples with hexameric helicase DnaB inBiophysics reports · 2025Article
- Structural basis of the T4 bacteriophage primosome assembly and primer synthesis.Nature communications · 2023Article
- Structural basis of the T4 bacteriophage primosome assembly and primer synthesis.bioRxiv : the preprint server for biology · 2023Article
- Theoretical Development of DnaG Primase as a Novel Narrow-Spectrum Antibiotic Target.ACS omega · 2022Article
- Quantitation of nucleoprotein complexes by UV absorbance and Bradford assay.Biophysics reports · 2021Article
- DnaG Primase-A Target for the Development of Novel Antibacterial Agents.Antibiotics (Basel, Switzerland) · 2018Review
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- Plant organellar DNA primase-helicase synthesizes RNA primers for organellar DNA polymerases using a unique recognition sequence.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial primase initiates the repeated synthesis of short RNA primers that are extended by DNA polymerase to synthesize Okazaki fragments on the lagging strand at replication forks. It remains unclear how the enzyme recognizes specific initiation sites. In this study, the DnaG primase from Bacillus subtilis (BsuDnaG) was characterized and the crystal structure of the RNA polymerase domain (RPD) was determined. Structural comparisons revealed that the tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. Structural and biochemical data defined the ssDNA template binding surface as an L shape, and a model for the template ssDNA binding to primase is proposed. The flexibility of the DnaG primases from B. subtilis and G. stearothermophilus were compared, and the results implied that the intrinsic flexibility of the primase may facilitate the interactions between primase and various partners in the replisome. These results shed light on the mechanism by which DnaG recognizes the specific initiation site.
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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.