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ATP half-sites in RadA and RAD51 recombinases bind nucleotides

DOI: 10.1002/2211-5463.12052 DOI Help

Authors: May E. Marsh (University of Cambridge) , Duncan E. Scott (University of Cambridge) , Matthias T. Ehebauer (University of Cambridge) , Chris Abell (University of Cambridge) , Tom L. Blundell (University of Cambridge) , Marko Hyvönen (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Open Bio

State: Published (Approved)
Published: March 2016
Diamond Proposal Number(s): 315

Open Access Open Access

Abstract: Homologous recombination is essential for repair of DNA double–strand breaks. Central to this process is a family of recombinases, including archeal RadA and human RAD51, which form nucleoprotein filaments on damaged single–stranded DNA ends and facilitate their ATP-dependent repair. ATP binding and hydrolysis are dependent on the formation of a nucleoprotein filament comprising RadA/RAD51 and single–stranded DNA, with ATP bound between adjacent protomers. We demonstrate that truncated, monomeric P. furiosus RadA and monomerised Human RAD51 retain the ability to bind ATP and other nucleotides with high affinity. We present crystal structures of both apo and nucleotide-bound forms of monomeric RadA. These structures reveal that whilst phosphate groups are tightly bound, RadA presents a shallow, poorly defined binding surface for the nitrogenous bases of nucleotides. We suggest that RadA monomers would be constitutively bound to nucleotides in the cell and that the bound nucleotide might play a structural role in filament assembly.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography

Other Facilities: ESRF; SLS

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