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Updated: Apr 20, 2026

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
Published on: June 26, 2020
Molecular architecture of the HerA-NurA DNA double-strand break resection complex
Robert Thomas Byrne1, Jan Michael Schuller2, Pia Unverdorben2
1Gene Center and Department of Biochemistry, Ludwig-Maximilians-University Munich, Feodor-Lynen-Straße 25, D-81377 Munich, Germany.
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.
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