title: Molecular architecture of the HerA-NurA DNA double-strand break resection complex.
abstract: DNA double-strand breaks can be repaired by homologous recombination, during which the DNA ends are long-range resected by helicase-nuclease systems to generate 3' single strand tails. In archaea, this requires the Mre11-Rad50 complex and the ATP-dependent helicase-nuclease complex HerA-NurA. We report the cryo-EM structure of Sulfolobus solfataricus HerA-NurA at 7.4Å resolution and present the pseudo-atomic model of the complex. HerA forms an ASCE hexamer that tightly interacts with a NurA dimer, with each NurA protomer binding three adjacent HerA HAS domains. Entry to NurA's nuclease active sites requires dsDNA to pass through a 23Å wide channel in the HerA hexamer. The structure suggests that HerA is a dsDNA translocase that feeds DNA into the NurA nuclease sites.
authors.affiliation: Gene Center and Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Straße 25, D-81377 Munich, Germany.
authors.forename: Robert Thomas
authors.initials: RT
authors.lastname: Byrne
authors.affiliation: Department of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
authors.forename: Jan Michael
authors.initials: JM
authors.lastname: Schuller
authors.affiliation: Department of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
authors.forename: Pia
authors.initials: P
authors.lastname: Unverdorben
authors.affiliation: Department of Molecular Structural Biology, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany. Electronic address: foerster@biochem.mpg.de.
authors.forename: Friedrich
authors.initials: F
authors.lastname: Förster
authors.affiliation: Gene Center and Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Straße 25, D-81377 Munich, Germany; Center for Integrated Protein Sciences, Munich, Germany. Electronic address: hopfner@genzentrum.lmu.de.
authors.forename: Karl-Peter
authors.initials: KP
authors.lastname: Hopfner
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D020134:Catalytic Domain; D004247:DNA / Q000235:genetics / Q000378:metabolism; D053903:DNA Breaks, Double-Stranded; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D048229:Sulfolobus solfataricus / Q000201:enzymology
chemical_list: D000255:Adenosine Triphosphate; D004247:DNA; D003851:Deoxyribonucleases; D004265:DNA Helicases
keywords: Cryo-electron microscopy; DNA double-strand break repair; DNA resection; FtsK/HerA ATPase; Nuclease