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

Rzechorzek, Neil J. and Blackwood, John K. and Bray, Sian M. and Maman, Joseph D. and Pellegrini, Luca and Robinson, Nicholas P. (2014) Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea. Nature Communications, 5. p. 5506. ISSN 2041-1723

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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.

Item Type:
Journal Article
Journal or Publication Title:
Nature Communications
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/3100
Subjects:
ID Code:
86205
Deposited By:
Deposited On:
04 May 2017 13:20
Refereed?:
Yes
Published?:
Published
Last Modified:
12 Aug 2020 06:11