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Molecular architecture of the HerA-NurA DNA double-strand break resection complex

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Schuller,  Jan Michael
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Unverdorben,  Pia
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Förster,  Friedrich
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Byrne, R. T., Schuller, J. M., Unverdorben, P., Förster, F., & Hopfner, K.-P. (2014). Molecular architecture of the HerA-NurA DNA double-strand break resection complex. FEBS LETTERS, 588(24), 4637-4644. doi:10.1016/j.febslet.2014.10.035.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-81D7-E
Zusammenfassung
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 30 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 angstrom 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 angstrom wide channel in the HerA hexamer. The structure suggests that HerA is a dsDNA translocase that feeds DNA into the NurA nuclease sites. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.