ArticleThe Journal of biological chemistry2013
The N-terminal 45-kDa domain of Dna2 endonuclease/helicase targets the enzyme to secondary structure DNA.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Creation and resolution of non-B-DNA structural impediments during replication.Critical reviews in biochemistry and molecular biology · 2022Article
- The secondary-structured DNA-binding activity of Dna2 endonuclease/helicase is critical to cell growth under replication stress.The FEBS journal · 2021Article
- The iron-sulphur cluster in human DNA2 is required for all biochemical activities of DNA2.Communications biology · 2020Article
- Sumoylation regulates the stability and nuclease activity ofCommunications biology · 2019Article
- hDNA2 nuclease/helicase promotes centromeric DNA replication and genome stability.The EMBO journal · 2018Article
- DNA2-An Important Player in DNA Damage Response or Just Another DNA Maintenance Protein?International journal of molecular sciences · 2017Review
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- Yet another job for Dna2: Checkpoint activation.DNA repair · 2015Review
- Borrowing nuclear DNA helicases to protect mitochondrial DNA.International journal of molecular sciences · 2015Review
- Rad52/Rad59-dependent recombination as a means to rectify faulty Okazaki fragment processing.The Journal of biological chemistry · 2014Article
- Mammalian DNA2 helicase/nuclease cleaves G-quadruplex DNA and is required for telomere integrity.The EMBO journal · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The removal of initiating primers from the 5'-ends of each Okazaki fragment, required for the generation of contiguous daughter strands, can be catalyzed by the combined action of DNA polymerase δ and Fen1. When the flaps generated by displacement of DNA synthesis activity of polymerase δ become long enough to bind replication protein A or form hairpin structures, the helicase/endonuclease enzyme, Dna2, becomes critical because of its ability to remove replication protein A-coated or secondary structure flaps. In this study, we show that the N-terminal 45-kDa domain of Dna2 binds hairpin structures, allowing the enzyme to target secondary structure flap DNA. We found that this activity was essential for the efficient removal of hairpin flaps by the endonuclease activity of Dna2 with the aid of its helicase activity. Thus, the efficient removal of hairpin structure flaps requires the coordinated action of all three functional domains of Dna2. We also found that deletion of the N-terminal 45-kDa domain of Dna2 led to a partial loss of the intra-S-phase checkpoint function and an increased rate of homologous recombination in yeast. We discuss the potential roles of the N-terminal domain of Dna2 in the maintenance of genomic stability.
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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.