ArticleBMC molecular biology2015
Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus.
Article in BMC molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Alkylated DNA repair by a novel HhH-GPD family protein from Crenarchaea.Nucleic acids research · 2025Article
- Article
- Article
- Archaeal DNA-import apparatus is homologous to bacterial conjugation machinery.Nature communications · 2023Article
- Sulfolobus islandicus Employs Orc1-2-Mediated DNA Damage Response in Defense against Infection by SSV2.Journal of virology · 2022Article
- 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
- Role of RadA and DNA Polymerases in Recombination-Associated DNA Synthesis in Hyperthermophilic Archaea.Biomolecules · 2020Article
- Genetic Control of Oxidative Mutagenesis inJournal of bacteriology · 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
- An Orc1/Cdc6 ortholog functions as a key regulator in the DNA damage response in Archaea.Nucleic acids research · 2018Article
- The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction.Nucleic acids research · 2018Article
- Physical and functional interplay between PCNA DNA clamp and Mre11-Rad50 complex from the archaeon Pyrococcus furiosus.Nucleic acids research · 2018Article
- Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Nucleic acids research · 2017Article
- Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.Journal of molecular biology · 2017Article
- Autophosphorylation and Cross-Phosphorylation of Protein Kinases from the CrenarchaeonFrontiers in microbiology · 2017Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundATPase/Helicases and nucleases play important roles in homologous recombination repair (HRR). Many of the mechanistic details relating to these enzymes and their function in this fundamental and complicated DNA repair process remain poorly understood in archaea. Here we employed Sulfolobus islandicus, a hyperthermophilic archaeon, as a model to investigate the in vivo functions of the ATPase/helicase HerA, the nuclease NurA, and their associated proteins Mre11 and Rad50.
resultsWe revealed that each of the four genes in the same operon, mre11, rad50, herA, and nurA, are essential for cell viability by a mutant propagation assay. A genetic complementation assay with mutant proteins was combined with biochemical characterization demonstrating that the ATPase activity of HerA, the interaction between HerA and NurA, and the efficient 5'-3' DNA end resection activity of the HerA-NurA complex are essential for cell viability. NurA and two other putative HRR proteins: a PIN (PilT N-terminal)-domain containing ATPase and the Holliday junction resolvase Hjc, were co-purified with a chromosomally encoded N-His-HerA in vivo. The interactions of HerA with the ATPase and Hjc were further confirmed by in vitro pull down.
conclusionEfficient 5'-3' DNA end resection activity of the HerA-NurA complex contributes to necessity of HerA and NurA in Sulfolobus, which is crucial to yield a 3'-overhang in HRR. HerA may have additional binding partners in cells besides NurA.
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