ArticleNucleic acids research2010
WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 54 citations in OpenAlex.
- HELZ-BRCA2 complex resolves R-loops to drive transcription-coupled homologous recombination.Nature communications · 2026Article
- A structural accessibility principle for LbuCas13a activation by noncontiguous DNA.Nucleic acids research · 2026Article
- The Zinc Finger Ran-Binding Protein 3 (ZRANB3): An Advanced Perspective.International journal of molecular sciences · 2026Review
- Targeting R-loops: diverse RNA helicases in R-loop resolution and their potential as targets for cancer therapy.Frontiers in cell and developmental biology · 2026Review
- Machine learning driven multiomics analysis identifies disulfidptosis associated molecular subtypes in ovarian cancer.Scientific reports · 2025Article
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- RNA biogenesis and RNA metabolism factors as R-loop suppressors: a hidden role in genome integrity.Genes & development · 2024Review
- ATR phosphorylates DHX9 at serine 321 to suppress R-loop accumulation upon genotoxic stress.Nucleic acids research · 2024Article
- Werner syndrome protein works as a dimer for unwinding and replication fork regression.Nucleic acids research · 2023Article
- Implications of Translesion DNA Synthesis Polymerases on Genomic Stability and Human Health.Molecular and cellular biology · 2023Article
- A pan-cancer analysis of the expression and molecular mechanism of DHX9 in human cancers.Frontiers in pharmacology · 2023Article
- Polymerase η Recruits DHX9 Helicase to Promote Replication across Guanine Quadruplex Structures.Journal of the American Chemical Society · 2022Article
- DHX9-dependent recruitment of BRCA1 to RNA promotes DNA end resection in homologous recombination.Nature communications · 2021Article
- Dynamically probing ATP-dependent RNA helicase A-assisted RNA structure conversion using single molecule fluorescence resonance energy transfer.Protein science : a publication of the Protein Society · 2021Article
- The enigmatic helicase DHX9 and its association with the hallmarks of cancer.Future science OA · 2020Review
- Article
- The hRPC62 subunit of human RNA polymerase III displays helicase activity.Nucleic acids research · 2019Article
- MRE11-RAD50-NBS1 promotes Fanconi Anemia R-loop suppression at transcription-replication conflicts.Nature communications · 2019Article
- A DHX9-lncRNA-MDM2 interaction regulates cell invasion and angiogenesis of cervical cancer.Cell death and differentiation · 2019Article
- Cellular RNA Helicase DHX9 Interacts with the Essential Epstein-Barr Virus (EBV) Protein SM and Restricts EBV Lytic Replication.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in the Werner gene promote the segmental progeroid Werner syndrome (WS) with increased genomic instability and cancer. The Werner gene encodes a DNA helicase (WRN) that can engage in direct protein-protein interactions with DHX9, also known as RNA helicase A or nuclear DNA helicase II, which represents an essential enzyme involved in transcription and DNA repair. By using several synthetic nucleic acid substrates we demonstrate that WRN preferably unwinds RNA-containing Okazaki fragment-like substrates suggesting a role in lagging strand maturation of DNA replication. In contrast, DHX9 preferably unwinds RNA-RNA and RNA-DNA substrates, but fails to unwind Okazaki fragment-like hybrids. We further show that the preferential unwinding of RNA-containing substrates by WRN is stimulated by DHX9 in vitro, both on Okazaki fragment-like hybrids and on RNA-containing 'chicken-foot' structures. Collectively, our results suggest that WRN and DHX9 may also cooperate in vivo, e.g. at ongoing and stalled replication forks. In the latter case, the cooperation between both helicases may serve to form and to dissolve Holliday junction-like intermediates of regressed replication forks.
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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.