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

Neil J. Rzechorzek, John K. Blackwood, Sian M. Bray, Joseph D. Maman, Luca Pellegrini () and Nicholas P. Robinson ()
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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

Nature Communications, 2014, vol. 5, issue 1, 1-15

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6506

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