Repository logo

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



Change log


Rzechorzek, Neil J 
Blackwood, John K 
Bray, Sian M 
Maman, Joseph D 


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.



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 Title

Nat Commun

Conference Name

Journal ISSN


Volume Title



Springer Science and Business Media LLC
Medical Research Council (G0701443)
Wellcome Trust (104641/Z/14/Z)
Wellcome Trust (084279/Z/07/A)
The SAXS data collection was supported by funding from the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement N°283570). Research in the N.P.R. laboratory is funded by the Medical Research Council [Career Development Award G0701443]. Research in the L.P. laboratory is funded by a Wellcome Trust Senior Fellowship Award in Basic Biomedical Sciences [grant number 08279/Z/07/Z]. Work in the L.P. and N.P.R. laboratories is also supported by an Isaac Newton Trust Research Grant, and S.M.B. is supported by a BBSRC Doctoral Training Grant.