ArticleThe Journal of biological chemistry2008
Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 45 citations in OpenAlex.
- Telomere C-Strand Fill-In Machinery: New Insights into the Human CST-DNA Polymerase Alpha-Primase Structures and Functions.Sub-cellular biochemistry · 2024Review
- Distinct RPA domains promote recruitment and the helicase-nuclease activities of Dna2.Nature communications · 2021Article
- Dynamic regulation of Pif1 acetylation is crucial to the maintenance of genome stability.Current genetics · 2021Review
- Multiple roles of DNA2 nuclease/helicase in DNA metabolism, genome stability and human diseases.Nucleic acids research · 2020Review
- Review
- Dna2 processes behind the fork long ssDNA flaps generated by Pif1 and replication-dependent strand displacement.Nature communications · 2018Article
- A Critical Role for Dna2 at Unwound Telomeres.Genetics · 2018Article
- Dynamic DNA binding, junction recognition and G4 melting activity underlie the telomeric and genome-wide roles of human CST.Nucleic acids research · 2017Article
- A novel role of the Dna2 translocase function in DNA break resection.Genes & development · 2017Article
- Dynamic binding of replication protein a is required for DNA repair.Nucleic acids research · 2016Article
- A Selective Small Molecule DNA2 Inhibitor for Sensitization of Human Cancer Cells to Chemotherapy.EBioMedicine · 2016Article
- Article
- Genetic Interactions Implicating Postreplicative Repair in Okazaki Fragment Processing.PLoS genetics · 2015Article
- The Saccharomyces cerevisiae Dna2 can function as a sole nuclease in the processing of Okazaki fragments in DNA replication.Nucleic acids research · 2015Article
- Sulfolobus chromatin proteins modulate strand displacement by DNA polymerase B1.Nucleic acids research · 2013Article
- Okazaki fragment metabolism.Cold Spring Harbor perspectives in biology · 2013Review
- Structure and conformational change of a replication protein A heterotrimer bound to ssDNA.Genes & development · 2012Article
- Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1.Nucleic acids research · 2012Article
- Okazaki fragment processing-independent role for human Dna2 enzyme during DNA replication.The Journal of biological chemistry · 2012Article
- Human nuclease/helicase DNA2 alleviates replication stress by promoting DNA end resection.Cancer research · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic Okazaki fragments are initiated by a RNA/DNA primer, which is removed before the fragments are joined. Polymerase delta displaces the primer into a flap for processing. Dna2 nuclease/helicase and flap endonuclease 1 (FEN1) are proposed to cleave the flap. The single-stranded DNA-binding protein, replication protein A (RPA), governs cleavage activity. Flap-bound RPA inhibits FEN1. This necessitates cleavage by Dna2, which is stimulated by RPA. FEN1 then cuts the remaining RPA-free flap to create a nick for ligation. Cleavage by Dna2 requires that it enter the 5'-end and track down the flap. Because Dna2 cleaves the RPA-bound flap, we investigated the mechanism by which Dna2 accesses the protein-coated flap for cleavage. Using a nuclease-defective Dna2 mutant, we showed that just binding of Dna2 dissociates the flap-bound RPA. Facile dissociation is specific to substrates with a genuine flap, and will not occur with an RPA-coated single strand. We also compared the cleavage patterns of Dna2 with and without RPA to better define RPA stimulation of Dna2. Stimulation derived from removal of DNA folding in the flap. Apparently, coordinated with its dissociation, RPA relinquishes the flap to Dna2 for tracking in a way that does not allow flap structure to reform. We also found that RPA strand melting activity promotes excessive flap elongation, but it is suppressed by Dna2-promoted RPA dissociation. Overall, results indicate that Dna2 and RPA coordinate their functions for efficient flap cleavage and preparation for FEN1.
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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.