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

Author

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  • Neil J. Rzechorzek

    (University of Cambridge)

  • John K. Blackwood

    (University of Cambridge)

  • Sian M. Bray

    (University of Cambridge)

  • Joseph D. Maman

    (University of Cambridge)

  • Luca Pellegrini

    (University of Cambridge)

  • Nicholas P. Robinson

    (University of Cambridge)

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.

Suggested Citation

  • Neil J. Rzechorzek & John K. Blackwood & Sian M. Bray & Joseph D. Maman & Luca Pellegrini & Nicholas P. Robinson, 2014. "Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea," Nature Communications, Nature, vol. 5(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6506
    DOI: 10.1038/ncomms6506
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    Cited by:

    1. Xiangkai Zhen & Biao Zhou & Zihe Liu & Xurong Wang & Heyu Zhao & Shuxian Wu & Zekai Li & Jiamin liang & Wanyue Zhang & Qingjian Zhu & Jun He & Xiaoli Xiong & Songying Ouyang, 2024. "Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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