ArticleNucleic acids research2012
Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex.
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 30 papers.
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Who cites it
30 citing papers in PubMed.
- Article
- The Deinococcus protease PprI senses DNA damage by directly interacting with single-stranded DNA.Nature communications · 2024Article
- Protocol for performing and optimizing differential scanning fluorimetry experiments.STAR protocols · 2023Article
- Article
- Archaeal DNA-import apparatus is homologous to bacterial conjugation machinery.Nature communications · 2023Article
- The Finely Coordinated Action of SSB and NurA/HerA Complex Strictly Regulates the DNA End Resection Process inInternational journal of molecular sciences · 2022Article
- Take a Break to Repair: A Dip in the World of Double-Strand Break Repair Mechanisms Pointing the Gaze on Archaea.International journal of molecular sciences · 2021Review
- Review
- Archaeal DNA Repair Mechanisms.Biomolecules · 2020Review
- Modes of action of the archaeal Mre11/Rad50 DNA-repair complex revealed by fast-scan atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phosphorylation of the Archaeal Holliday Junction Resolvase Hjc Inhibits Its Catalytic Activity and Facilitates DNA Repair inFrontiers in microbiology · 2019Article
- Resistance to UV Irradiation Caused by Inactivation ofJournal of bacteriology · 2018Article
- The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity.Extremophiles : life under extreme conditions · 2018Article
- Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Nucleic acids research · 2017Article
- Coupling transcriptional activation of CRISPR-Cas system and DNA repair genes by Csa3a in Sulfolobus islandicus.Nucleic acids research · 2017Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- The transjugation machinery of Thermus thermophilus: Identification of TdtA, an ATPase involved in DNA donation.PLoS genetics · 2017Article
- The archaeal Ced system imports DNA.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Biochemical and Functional Characterization of the NurA-HerA Complex from Deinococcus radiodurans.Journal of bacteriology · 2015Article
- Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus.BMC molecular biology · 2015Article
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6 authors.
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Abstract
Helicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex.
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