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Molecular architecture of the HerA–NurA DNA double‐strand break resection complex
Author(s) -
Byrne Robert Thomas,
Schuller Jan Michael,
Unverdorben Pia,
Förster Friedrich,
Hopfner Karl-Peter
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.10.035
Subject(s) - hera , nuclease , random hexamer , helicase , sulfolobus solfataricus , homologous recombination , dna , biology , chemistry , genetics , microbiology and biotechnology , physics , gene , archaea , rna , particle physics , quantum chromodynamics
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 7.4 Å 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 23 Å wide channel in the HerA hexamer. The structure suggests that HerA is a dsDNA translocase that feeds DNA into the NurA nuclease sites.