ArticleEMBO reports2022
Structural mechanism underpinning Thermus oshimai Pif1-mediated G-quadruplex unfolding.
Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 16 citations in OpenAlex.
- Cryo-EM structures of human FANCJ reveal the mechanism of G-quadruplex unwinding and disease-associated mutations.Nature communications · 2026Article
- G-Quadruplex Unwinding Molecular Mechanisms by Helicases and Their Applications.International journal of molecular sciences · 2026Review
- Non-B DNA structures and their contributions to genetic diversity, aging, and disease.Nucleic acids research · 2026Review
- Structural basis of G-quadruplex recognition by a camelid antibody fragment.Nucleic acids research · 2025Article
- Structural basis for nucleolin recognition ofScience (New York, N.Y.) · 2025Article
- Effects of hydrazone-based G-quadruplex ligands onNAR cancer · 2025Article
- Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025Review
- A Compendium of G-Flipon Biological Functions That Have Experimental Validation.International journal of molecular sciences · 2024Review
- Eukaryotic Pif1 helicase unwinds G-quadruplex and dsDNA using a conserved wedge.Nature communications · 2024Article
- Structural Motifs at the Telomeres and Their Role in Regulatory Pathways.Biochemistry · 2024Review
- Exploring the G-quadruplex binding and unwinding activity of the bacterial FeS helicase DinG.Scientific reports · 2023Article
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- Structural mechanism underpinning Thermus oshimai Pif1-mediated G-quadruplex unfolding.EMBO reports · 2022Article
- The Cellular Functions and Molecular Mechanisms of G-Quadruplex Unwinding Helicases in Humans.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-quadruplexes (G4s) are unusual stable DNA structures that cause genomic instability. To overcome the potential barriers formed by G4s, cells have evolved different families of proteins that unfold G4s. Pif1 is a DNA helicase from superfamily 1 (SF1) conserved from bacteria to humans with high G4-unwinding activity. Here, we present the first X-ray crystal structure of the Thermus oshimai Pif1 (ToPif1) complexed with a G4. Our structure reveals that ToPif1 recognizes the entire native G4 via a cluster of amino acids at domains 1B/2B which constitute a G4-Recognizing Surface (GRS). The overall structure of the G4 maintains its three-layered propeller-type G4 topology, without significant reorganization of G-tetrads upon protein binding. The three G-tetrads in G4 are recognized by GRS residues mainly through electrostatic, ionic interactions, and hydrogen bonds formed between the GRS residues and the ribose-phosphate backbone. Compared with previously solved structures of SF2 helicases in complex with G4, our structure reveals how helicases from distinct superfamilies adopt different strategies for recognizing and unfolding G4s.
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