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

Robert Thomas Byrne; Jan Michael Schuller; Pia Unverdorben; Friedrich Förster; Karl-Peter Hopfner

doi:10.1016/j.febslet.2014.10.035

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

Robert Thomas Byrne, Jan Michael Schuller, Pia Unverdorben, Friedrich Förster, Karl-Peter Hopfner

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Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	4637-44
Number of pages	8
Journal	FEBS Letters
Volume	588
Issue number	24
DOIs	https://doi.org/10.1016/j.febslet.2014.10.035
Publication status	Published - 20 Dec 2014
Externally published	Yes

Keywords

Adenosine Triphosphate
Catalytic Domain
DNA
DNA Breaks, Double-Stranded
DNA Helicases
Deoxyribonucleases
Models, Molecular
Protein Multimerization
Protein Structure, Quaternary
Sulfolobus solfataricus

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10.1016/j.febslet.2014.10.035

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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 7.4{\AA} 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{\AA} wide channel in the HerA hexamer. The structure suggests that HerA is a dsDNA translocase that feeds DNA into the NurA nuclease sites.",

keywords = "Adenosine Triphosphate, Catalytic Domain, DNA, DNA Breaks, Double-Stranded, DNA Helicases, Deoxyribonucleases, Models, Molecular, Protein Multimerization, Protein Structure, Quaternary, Sulfolobus solfataricus",

author = "Byrne, \{Robert Thomas\} and Schuller, \{Jan Michael\} and Pia Unverdorben and Friedrich F{\"o}rster and Karl-Peter Hopfner",

year = "2014",

month = dec,

day = "20",

doi = "10.1016/j.febslet.2014.10.035",

language = "English",

volume = "588",

pages = "4637--44",

journal = "FEBS Letters",

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TY - JOUR

T1 - Molecular architecture of the HerA-NurA DNA double-strand break resection complex

AU - Byrne, Robert Thomas

AU - Schuller, Jan Michael

AU - Unverdorben, Pia

AU - Förster, Friedrich

AU - Hopfner, Karl-Peter

PY - 2014/12/20

Y1 - 2014/12/20

N2 - 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.

AB - 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.

KW - Adenosine Triphosphate

KW - Catalytic Domain

KW - DNA

KW - DNA Breaks, Double-Stranded

KW - DNA Helicases

KW - Deoxyribonucleases

KW - Models, Molecular

KW - Protein Multimerization

KW - Protein Structure, Quaternary

KW - Sulfolobus solfataricus

U2 - 10.1016/j.febslet.2014.10.035

DO - 10.1016/j.febslet.2014.10.035

M3 - Article

C2 - 25447518

SN - 0014-5793

VL - 588

SP - 4637

EP - 4644

JO - FEBS Letters

JF - FEBS Letters

IS - 24

ER -

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

Abstract

Keywords

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