ArticleScientific reports2018
ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.
Article in Scientific reports, 2018. 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 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.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Illustration of the variable 1D sequences but conserved 2D and 3D structures of different ncRNA nanostructures for tracking the evolution and origin of organisms.Non-coding RNA research · 2026Article
- The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025Review
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- RecF protein targeting to postreplication (daughter strand) gaps I: DNA binding by RecF and RecFR.Nucleic acids research · 2023Article
- RecF protein targeting to post-replication (daughter strand) gaps II: RecF interaction with replisomes.Nucleic acids research · 2023Article
- Mechanism of RecF-RecO-RecR cooperation in bacterial homologous recombination.Nature structural & molecular biology · 2023Article
- The ATP-dependent Pathways and Human Diseases.Current medicinal chemistry · 2023Article
- Review
- A Review of the Functional Annotations of Important Genes in the AHPND-Causing pVA1 Plasmid.Microorganisms · 2020Review
- The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases.Nucleic acids research · 2020Article
- Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin.Molecular cell · 2019Article
- RecFOR epistasis group: RecF and RecO have distinct localizations and functions in Escherichia coli.Nucleic acids research · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization and structural homology with Rad50 and SMC proteins. However, the mechanism and action pattern of RecF ATP-dependent dimerization remains unclear. Here, We determined three crystal structures of TTERecF, TTERecF-ATP and TTERecF-ATPɤS from Thermoanaerobacter tengcongensis that reveal a novel ATP-driven RecF dimerization. RecF contains a positively charged tunnel on its dimer interface that is essential to ATP binding. Our structural and biochemical data indicate that the Walker A motif serves as a switch and plays a key role in ATP binding and RecF dimerization. Furthermore, Biolayer interferometry assay results showed that the TTERecF interacted with ATP and formed a dimer, displaying a higher affinity for DNA than that of the TTERecF monomer. Overall, our results provide a solid structural basis for understanding the process of RecF binding with ATP and the functional mechanism of ATP-dependent RecF dimerization.
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