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Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea

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Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. / Rzechorzek, Neil J.; Blackwood, John K.; Bray, Sian M. et al.

In: Nature Communications, Vol. 5, 25.11.2014, p. 5506.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Rzechorzek, NJ, Blackwood, JK, Bray, SM, Maman, JD, Pellegrini, L & Robinson, NP 2014, 'Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea', Nature Communications, vol. 5, pp. 5506. https://doi.org/10.1038/ncomms6506

APA

Rzechorzek, N. J., Blackwood, J. K., Bray, S. M., Maman, J. D., Pellegrini, L., & Robinson, N. P. (2014). Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nature Communications, 5, 5506. https://doi.org/10.1038/ncomms6506

Vancouver

Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP. Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nature Communications. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506

Author

Rzechorzek, Neil J. ; Blackwood, John K. ; Bray, Sian M. et al. / Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. In: Nature Communications. 2014 ; Vol. 5. pp. 5506.

Bibtex

@article{7eb939b9f1f3424091d1d5a055ab4f29,
title = "Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea",
abstract = "The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.",
keywords = "Adenosine Triphosphatases, Amino Acid Sequence, Archaea, Archaeal Proteins, DNA Breaks, Double-Stranded, DNA, Archaeal, Deoxyribonucleases, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Translocation, Genetic, Journal Article, Research Support, Non-U.S. Gov't",
author = "Rzechorzek, {Neil J.} and Blackwood, {John K.} and Bray, {Sian M.} and Maman, {Joseph D.} and Luca Pellegrini and Robinson, {Nicholas P.}",
year = "2014",
month = nov,
day = "25",
doi = "10.1038/ncomms6506",
language = "English",
volume = "5",
pages = "5506",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea

AU - Rzechorzek, Neil J.

AU - Blackwood, John K.

AU - Bray, Sian M.

AU - Maman, Joseph D.

AU - Pellegrini, Luca

AU - Robinson, Nicholas P.

PY - 2014/11/25

Y1 - 2014/11/25

N2 - The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.

AB - The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine.

KW - Adenosine Triphosphatases

KW - Amino Acid Sequence

KW - Archaea

KW - Archaeal Proteins

KW - DNA Breaks, Double-Stranded

KW - DNA, Archaeal

KW - Deoxyribonucleases

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Translocation, Genetic

KW - Journal Article

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

U2 - 10.1038/ncomms6506

DO - 10.1038/ncomms6506

M3 - Journal article

C2 - 25420454

VL - 5

SP - 5506

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -