ArticleNucleic acids research2014
Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Single-molecule studies of repair proteins in base excision repair.BMB reports · 2025Review
- Mechanistic investigation of human maturation of Okazaki fragments reveals slow kinetics.Nature communications · 2022Article
- Structural dynamics of DNA strand break sensing by PARP-1 at a single-molecule level.Nature communications · 2022Article
- Cas1 and Fen1 Display Equivalent Functions During Archaeal DNA Repair.Frontiers in microbiology · 2022Article
- Implementing fluorescence enhancement, quenching, and FRET for investigating flap endonuclease 1 enzymatic reaction at the single-molecule level.Computational and structural biotechnology journal · 2021Review
- Sulfamethoxazole-Altered Transcriptomein Green AlgaFrontiers in microbiology · 2021Article
- Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation.Nature communications · 2020Article
- Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase.Nucleic acids research · 2019Article
- Initial state of DNA-Dye complex sets the stage for protein induced fluorescence modulation.Nature communications · 2019Article
- Missed cleavage opportunities by FEN1 lead to Okazaki fragment maturation via the long-flap pathway.Nucleic acids research · 2018Article
- Positioning the 5'-flap junction in the active site controls the rate of flap endonuclease-1-catalyzed DNA cleavage.The Journal of biological chemistry · 2018Article
- Characterizing highly dynamic conformational states: The transcription bubble in RNAP-promoter open complex as an example.The Journal of chemical physics · 2018Article
- Interacting partners of FEN1 and its role in the development of anticancer therapeutics.Oncotarget · 2017Review
- High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein.Extremophiles : life under extreme conditions · 2017Article
- Single-molecule FRET unveils induced-fit mechanism for substrate selectivity in flap endonuclease 1.eLife · 2017Article
- Cloning, recombinant production and crystallographic structure of Proliferating Cell Nuclear Antigen from radioresistant archaeonBiochemistry and biophysics reports · 2016Review
- Cellularly active N-hydroxyurea FEN1 inhibitors block substrate entry to the active site.Nature chemical biology · 2016Article
- Förster resonance energy transfer and protein-induced fluorescence enhancement as synergetic multi-scale molecular rulers.Scientific reports · 2016Article
- A Quantitative Theoretical Framework For Protein-Induced Fluorescence Enhancement-Förster-Type Resonance Energy Transfer (PIFE-FRET).The journal of physical chemistry. B · 2016Article
- DNA and Protein Requirements for Substrate Conformational Changes Necessary for Human Flap Endonuclease-1-catalyzed Reaction.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Flap endonuclease 1 (Fen1) is a highly conserved structure-specific nuclease that catalyses a specific incision to remove 5' flaps in double-stranded DNA substrates. Fen1 plays an essential role in key cellular processes, such as DNA replication and repair, and mutations that compromise Fen1 expression levels or activity have severe health implications in humans. The nuclease activity of Fen1 and other FEN family members can be stimulated by processivity clamps such as proliferating cell nuclear antigen (PCNA); however, the exact mechanism of PCNA activation is currently unknown. Here, we have used a combination of ensemble and single-molecule Förster resonance energy transfer together with protein-induced fluorescence enhancement to uncouple and investigate the substrate recognition and catalytic steps of Fen1 and Fen1/PCNA complexes. We propose a model in which upon Fen1 binding, a highly dynamic substrate is bent and locked into an open flap conformation where specific Fen1/DNA interactions can be established. PCNA enhances Fen1 recognition of the DNA substrate by further promoting the open flap conformation in a step that may involve facilitated threading of the 5' ssDNA flap. Merging our data with existing crystallographic and molecular dynamics simulations we provide a solution-based model for the Fen1/PCNA/DNA ternary complex.
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Registered trials
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.