ArticleNucleic acids research2012
Cross talk between the nuclease and helicase activities of Dna2: role of an essential iron-sulfur cluster domain.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 52 citations in OpenAlex.
- Iron-sulfur cofactors in nucleic acid metabolism and protein synthesis: Assembly, delivery, and putative roles in cellular and viral systems.The Journal of biological chemistry · 2026Review
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Biochemical Mechanisms of Genetic Recombination and DNA Repair.Annual review of biochemistry · 2025Review
- Control of Replication Stress Response by Cytosolic Fe-S Cluster Assembly (CIA) Machinery.Cells · 2025Review
- Dna2 removes toxic ssDNA-RPA filaments generated from meiotic recombination-associated DNA synthesis.Nucleic acids research · 2023Article
- Maintenance of genome integrity by the late-acting cytoplasmic iron-sulfur assembly (CIA) complex.Frontiers in genetics · 2023Review
- Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei.Metallomics : integrated biometal science · 2022Article
- EXO5-DNA structure and BLM interactions direct DNA resection critical for ATR-dependent replication restart.Molecular cell · 2021Article
- Fungal-Metal Interactions: A Review of Toxicity and Homeostasis.Journal of fungi (Basel, Switzerland) · 2021Review
- Implications of Membrane Binding by the Fe-S Cluster-Containing N-Terminal Domain in theFrontiers in genetics · 2021Article
- Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021Review
- Decoding Cancer Variants of Unknown Significance for Helicase-Nuclease-RPA Complexes Orchestrating DNA Repair During Transcription and Replication.Frontiers in molecular biosciences · 2021Article
- Bulk and single-molecule analysis of a bacterial DNA2-like helicase-nuclease reveals a single-stranded DNA looping motor.Nucleic acids research · 2020Article
- Structural insights into Fe-S protein biogenesis by the CIA targeting complex.Nature structural & molecular biology · 2020Article
- UvrC Coordinates an OJournal of the American Chemical Society · 2020Article
- The iron-sulphur cluster in human DNA2 is required for all biochemical activities of DNA2.Communications biology · 2020Article
- Multiple roles of DNA2 nuclease/helicase in DNA metabolism, genome stability and human diseases.Nucleic acids research · 2020Review
- A comprehensive mechanistic model of iron metabolism in Saccharomyces cerevisiae.Metallomics : integrated biometal science · 2019Article
- The roles of fission yeast exonuclease 5 in nuclear and mitochondrial genome stability.DNA repair · 2019Article
- Redox Chemistry in the Genome: Emergence of the [4Fe4S] Cofactor in Repair and Replication.Annual review of biochemistry · 2019Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dna2 nuclease/helicase is a multitasking protein involved in DNA replication and recombinational repair, and it is important for preservation of genomic stability. Yeast Dna2 protein contains a conserved putative Fe-S (iron-sulfur) cluster signature motif spanning the nuclease active site. We show that this motif is indeed an Fe-S cluster domain. Mutation of cysteines involved in metal coordination greatly reduces not just the nuclease activity but also the ATPase activity of Dna2, suggesting that the nuclease and helicase activities are coupled. The affinity for DNA is not significantly reduced, but binding mode in the C to A mutants is altered. Remarkably, a point mutation (P504S), proximal to the Fe-S cluster domain, which renders cells temperature sensitive, closely mimics the global defects of the Fe-S cluster mutation itself. This points to an important role of this conserved proline residue in stabilizing the Fe-S cluster. The C to A mutants are deficient in DNA replication and repair in vivo, and, strikingly, the degree to which they are defective correlates directly with degree of loss of enzymatic activity. Taken together with previous results showing that mutations in the ATP domain affect nuclease function, our results provide a new mechanistic paradigm for coupling between nuclease and helicase modules fused in the same polypeptide.
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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.