Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex

Blackwood, John K. and Rzechorzek, Neil J. and Abrams, Andrew S. and Maman, Joseph D. and Pellegrini, Luca and Robinson, Nicholas P. (2012) Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex. Nucleic Acids Research, 40 (7). pp. 3183-96. ISSN 0305-1048

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Abstract

Helicase-nuclease systems dedicated to DNA end resection in preparation for homologous recombination (HR) are present in all kingdoms of life. In thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during HR-dependent DNA repair. Here we show that HerA and NurA must interact in a complex with specific subunit stoichiometry to process DNA ends efficiently. We determine crystallographically that NurA folds in a toroidal dimer of intertwined RNaseH-like domains. The central channel of the NurA dimer is too narrow for double-stranded DNA but appears well suited to accommodate one or two strands of an unwound duplex. We map a critical interface of the complex to an exposed hydrophobic epitope of NurA abutting the active site. Based upon the presented evidence, we propose alternative mechanisms of DNA end processing by the HerA-NurA complex.

Item Type: Journal Article
Journal or Publication Title: Nucleic Acids Research
Uncontrolled Keywords: /dk/atira/pure/subjectarea/asjc/1300/1311
Subjects:
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 86192
Deposited By: ep_importer_pure
Deposited On: 04 May 2017 09:08
Refereed?: Yes
Published?: Published
Last Modified: 01 Jan 2020 10:19
URI: https://eprints.lancs.ac.uk/id/eprint/86192

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