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Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex

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Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. / Blackwood, John K.; Rzechorzek, Neil J.; Abrams, Andrew S. et al.

In: Nucleic Acids Research, Vol. 40, No. 7, 04.2012, p. 3183-96.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Blackwood, JK, Rzechorzek, NJ, Abrams, AS, Maman, JD, Pellegrini, L & Robinson, NP 2012, 'Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex', Nucleic Acids Research, vol. 40, no. 7, pp. 3183-96. https://doi.org/10.1093/nar/gkr1157

APA

Blackwood, J. K., Rzechorzek, N. J., Abrams, A. S., Maman, J. D., Pellegrini, L., & Robinson, N. P. (2012). Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. Nucleic Acids Research, 40(7), 3183-96. https://doi.org/10.1093/nar/gkr1157

Vancouver

Blackwood JK, Rzechorzek NJ, Abrams AS, Maman JD, Pellegrini L, Robinson NP. Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. Nucleic Acids Research. 2012 Apr;40(7):3183-96. Epub 2011 Nov 30. doi: 10.1093/nar/gkr1157

Author

Blackwood, John K. ; Rzechorzek, Neil J. ; Abrams, Andrew S. et al. / Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. In: Nucleic Acids Research. 2012 ; Vol. 40, No. 7. pp. 3183-96.

Bibtex

@article{c62b4ca4f057484b8c84263c7cacac39,
title = "Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex",
abstract = "Helicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex.",
keywords = "Adenosine Triphosphate, Amino Acid Sequence, Archaeal Proteins, Conserved Sequence, Crystallography, X-Ray, DNA, DNA Helicases, Deoxyribonucleases, Dimerization, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Tertiary, Ribonuclease H, Sulfolobus solfataricus, Journal Article, Research Support, Non-U.S. Gov't",
author = "Blackwood, {John K.} and Rzechorzek, {Neil J.} and Abrams, {Andrew S.} and Maman, {Joseph D.} and Luca Pellegrini and Robinson, {Nicholas P.}",
year = "2012",
month = apr,
doi = "10.1093/nar/gkr1157",
language = "English",
volume = "40",
pages = "3183--96",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "7",

}

RIS

TY - JOUR

T1 - Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex

AU - Blackwood, John K.

AU - Rzechorzek, Neil J.

AU - Abrams, Andrew S.

AU - Maman, Joseph D.

AU - Pellegrini, Luca

AU - Robinson, Nicholas P.

PY - 2012/4

Y1 - 2012/4

N2 - Helicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex.

AB - Helicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex.

KW - Adenosine Triphosphate

KW - Amino Acid Sequence

KW - Archaeal Proteins

KW - Conserved Sequence

KW - Crystallography, X-Ray

KW - DNA

KW - DNA Helicases

KW - Deoxyribonucleases

KW - Dimerization

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Folding

KW - Protein Structure, Tertiary

KW - Ribonuclease H

KW - Sulfolobus solfataricus

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1093/nar/gkr1157

DO - 10.1093/nar/gkr1157

M3 - Journal article

C2 - 22135300

VL - 40

SP - 3183

EP - 3196

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 7

ER -