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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-81D7-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-81D8-C
Genre: Journal Article

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 Creators:
Byrne, Robert Thomas1, Author
Schuller, Jan Michael2, 3, Author              
Unverdorben, Pia2, 3, Author              
Förster, Friedrich2, 3, Author              
Hopfner, Karl-Peter1, Author
Affiliations:
1external, ou_persistent22              
2Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
3Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, Am Klopferspitz 18, 82152 Martinsried, DE, ou_1565142              

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Free keywords: ELECTRON-MICROSCOPY, END-RESECTION, CRYOELECTRON MICROSCOPY, THERMOPHILIC ARCHAEA, CRYSTAL-STRUCTURE, NUCLEASE COMPLEX, CHI RECOGNITION, RECBCD ENZYME, CRYO-EM, HELICASEBiochemistry & Molecular Biology; Biophysics; DNA double-strand break repair, Cryo-electron microscopy, Nuclease, DNA resection, FtsK/HerA ATPase;
 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 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.

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Language(s): eng - English
 Dates: 2014-12
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: FEBS LETTERS
Source Genre: Journal
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Publ. Info: PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS : ELSEVIER SCIENCE BV
Pages: - Volume / Issue: 588 (24) Sequence Number: - Start / End Page: 4637 - 4644 Identifier: ISSN: 0014-5793