ArticleNucleic acids research2014
Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Visualization of the complete preprimosome reveals the structural mechanisms governing DNA replication restart.Nature communications · 2026Article
- Visualization of the complete primosome reveals the structural mechanisms governing DNA replication restart.bioRxiv : the preprint server for biology · 2026Article
- Structural Analysis ofMolecules (Basel, Switzerland) · 2021Article
- Characterization of the Chimeric PriB-SSBc Protein.International journal of molecular sciences · 2021Article
- Function of a strand-separation pin element in the PriA DNA replication restart helicase.The Journal of biological chemistry · 2019Article
- Mechanisms of bacterial DNA replication restart.Nucleic acids research · 2018Review
- Structure-based domain assignment in Leishmania infantum EndoG: characterization of a pH-dependent regulatory switch and a C-terminal extension that largely dictates DNA substrate preferences.Nucleic acids research · 2017Article
- Staphylococcus aureus single-stranded DNA-binding protein SsbA can bind but cannot stimulate PriA helicase.PloS one · 2017Article
- RecG Directs DNA Synthesis during Double-Strand Break Repair.PLoS genetics · 2016Article
- A Replisome's journey through the bacterial chromosome.Frontiers in microbiology · 2015Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DnaT is a primosomal protein that is required for the stalled replication fork restart in Escherichia coli. As an adapter, DnaT mediates the PriA-PriB-ssDNA ternary complex and the DnaB/C complex. However, the fundamental function of DnaT during PriA-dependent primosome assembly is still a black box. Here, we report the 2.83 Å DnaT(84-153)-dT10 ssDNA complex structure, which reveals a novel three-helix bundle single-stranded DNA binding mode. Based on binding assays and negative-staining electron microscopy results, we found that DnaT can bind to phiX 174 ssDNA to form nucleoprotein filaments for the first time, which indicates that DnaT might function as a scaffold protein during the PriA-dependent primosome assembly. In combination with biochemical analysis, we propose a cooperative mechanism for the binding of DnaT to ssDNA and a possible model for the assembly of PriA-PriB-ssDNA-DnaT complex that sheds light on the function of DnaT during the primosome assembly and stalled replication fork restart. This report presents the first structure of the DnaT C-terminal complex with ssDNA and a novel model that explains the interactions between the three-helix bundle and ssDNA.
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