ArticleNucleic acids research2010
PCNA and XPF cooperate to distort DNA substrates.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Revisiting the Function of p21International journal of molecular sciences · 2022Review
- Review
- Substrate conformational dynamics facilitate structure-specific recognition of gapped DNA by DNA polymerase.Nucleic acids research · 2019Article
- Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork.Molecular cell · 2017Review
- Direct observation of DNA threading in flap endonuclease complexes.Nature structural & molecular biology · 2016Article
- Fluorescence-Based Strategies to Investigate the Structure and Dynamics of Aptamer-Ligand Complexes.Frontiers in chemistry · 2016Review
- Binding dynamics of a monomeric SSB protein to DNA: a single-molecule multi-process approach.Nucleic acids research · 2015Article
- Article
- The Mus81-Mms4 structure-selective endonuclease requires nicked DNA junctions to undergo conformational changes and bend its DNA substrates for cleavage.Nucleic acids research · 2014Article
- Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates.Nucleic acids research · 2014Article
- Characterization of the human SNM1A and SNM1B/Apollo DNA repair exonucleases.The Journal of biological chemistry · 2012Article
- Fluorescence-based incision assay for human XPF-ERCC1 activity identifies important elements of DNA junction recognition.Nucleic acids research · 2012Article
- Deficient expression of DNA repair enzymes in early progression to sporadic colon cancer.Genome integrity · 2012Article
- The wonders of flap endonucleases: structure, function, mechanism and regulation.Sub-cellular biochemistry · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
XPF is a structure-specific endonuclease that preferentially cleaves 3' DNA flaps during a variety of repair processes. The crystal structure of a crenarchaeal XPF protein bound to a DNA duplex yielded insights into how XPF might recognise branched DNA structures, and recent kinetic data have demonstrated that the sliding clamp PCNA acts as an essential cofactor, possibly by allowing XPF to distort the DNA structure into a proper conformation for efficient cleavage to occur. Here, we investigate the solution structure of the 3'-flap substrate bound to XPF in the presence and absence of PCNA using intramolecular Förster resonance energy transfer (FRET). We demonstrate that recognition of the flap substrate by XPF involves major conformational changes of the DNA, including a 90 degrees kink of the DNA duplex and organization of the single-stranded flap. In the presence of PCNA, there is a further substantial reorganization of the flap substrate bound to XPF, providing a structural basis for the observation that PCNA has an essential catalytic role in this system. The wider implications of these observations for the plethora of PCNA-dependent enzymes are discussed.
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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.