ArticleThe Journal of biological chemistry2010
Dna2 exhibits a unique strand end-dependent helicase function.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- The secondary-structured DNA-binding activity of Dna2 endonuclease/helicase is critical to cell growth under replication stress.The FEBS journal · 2021Article
- Bulk and single-molecule analysis of a bacterial DNA2-like helicase-nuclease reveals a single-stranded DNA looping motor.Nucleic acids research · 2020Article
- CtIP promotes the motor activity of DNA2 to accelerate long-range DNA end resection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Multiple roles of DNA2 nuclease/helicase in DNA metabolism, genome stability and human diseases.Nucleic acids research · 2020Review
- Competing interaction partners modulate the activity of Sgs1 helicase during DNA end resection.The EMBO journal · 2019Article
- Sumoylation regulates the stability and nuclease activity ofCommunications biology · 2019Article
- Dna2 initiates resection at clean DNA double-strand breaks.Nucleic acids research · 2017Article
- DNA2-An Important Player in DNA Damage Response or Just Another DNA Maintenance Protein?International journal of molecular sciences · 2017Review
- Article
- The motor activity of DNA2 functions as an ssDNA translocase to promote DNA end resection.Genes & development · 2017Article
- A novel role of the Dna2 translocase function in DNA break resection.Genes & development · 2017Article
- Article
- A Selective Small Molecule DNA2 Inhibitor for Sensitization of Human Cancer Cells to Chemotherapy.EBioMedicine · 2016Article
- Yet another job for Dna2: Checkpoint activation.DNA repair · 2015Review
- Exonuclease of human DNA polymerase gamma disengages its strand displacement function.Mitochondrion · 2013Article
- Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Flap endonuclease 1.Annual review of biochemistry · 2013Review
- Cross talk between the nuclease and helicase activities of Dna2: role of an essential iron-sulfur cluster domain.Nucleic acids research · 2012Article
- Article
- Characterization of the endonuclease and ATP-dependent flap endo/exonuclease of Dna2.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Dna2 endonuclease/helicase participates in eukaryotic DNA transactions including cleavage of long flaps generated during Okazaki fragment processing. Its unusual substrate interaction consists of recognition and binding of the flap base, then threading over the 5'-end of the flap, and cleaving periodically to produce a terminal product ∼5 nt in length. Blocking the 5'-end prevents cleavage. The Dna2 ATP-driven 5' to 3' DNA helicase function promotes motion of Dna2 on the flap, presumably aiding its nuclease function. Here we demonstrate using two different nuclease-dead Dna2 mutants that on substrates simulating Okazaki fragments, Dna2 must thread onto an unblocked 5' flap to display helicase activity. This requirement is maintained on substrates with single-stranded regions thousands of nucleotides in length. To our knowledge this is the first description of a eukaryotic helicase that cannot load onto its tracking strand internally but instead must enter from the end. Biologically, the loading requirement likely helps the helicase to coordinate with the Dna2 nuclease function to prevent creation of undesirably long flaps during DNA transactions.
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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.