ArticleProceedings of the National Academy of Sciences of the United States of America2022
The convergence of head-on DNA unwinding forks induces helicase oligomerization and activity transition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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.
- Cryo-EM structures of human FANCJ reveal the mechanism of G-quadruplex unwinding and disease-associated mutations.Nature communications · 2026Article
- RPA-ssDNA co-phase separation facilitates RAD51 enrichment during homologous recombination.Nucleic acids research · 2026Article
- VGLL4-driven TEAD4 multimerization orchestrates DNA binding and YAP recruitment.Nature communications · 2026Article
- HOP2-MND1 chaperones a diffusing DMC1-ssDNA complex to survey dsDNA for homology recognition during meiotic recombination.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Review
- RPA transforms RNase H1 to a bidirectional exoribonuclease for processive RNA-DNA hybrid cleavage.Nature communications · 2024Article
- Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex.Nucleic acids research · 2024Article
- Joint Efforts of Replicative Helicase and SSB Ensure Inherent Replicative Tolerance of G-Quadruplex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- RNase H1 facilitates recombinase recruitment by degrading DNA-RNA hybrids during meiosis.Nucleic acids research · 2023Article
- Stochastically multimerized ParB orchestrates DNA assembly as unveiled by single-molecule analysis.Nucleic acids research · 2022Article
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Authors and funding
10 authors.
Funding
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Abstract
Helicases are multifunctional motor proteins with the primary task of separating nucleic acid duplexes. These enzymes often exist in distinct oligomeric forms and play essential roles during nucleic acid metabolism. Whether there is a correlation between their oligomeric state and cellular function, and how helicases effectively perform functional switching remains enigmatic. Here, we address these questions using a combined single-molecule approach and Bloom syndrome helicase (BLM). By examining the head-on collision of two BLM-mediated DNA unwinding forks, we find that two groups of BLM, upon fork convergence, promptly oligomerize across the fork junctions and tightly bridge two independent single-stranded (ss) DNA molecules that were newly generated by the unwinding BLMs. This protein oligomerization is mediated by the helicase and RNase D C-terminal (HRDC) domain of BLM and can sustain a disruptive force of up to 300 pN. Strikingly, onsite BLM oligomerization gives rise to an immediate transition of their helicase activities, from unwinding dsDNA to translocating along ssDNA at exceedingly fast rates, thus allowing for the efficient displacement of ssDNA-binding proteins, such as RPA and RAD51. These findings uncover an activity transition pathway for helicases and help to explain how BLM plays both pro- and anti-recombination roles in the maintenance of genome stability.
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