Journal article

Inter-subunit interactions that coordinate Rad51s activities

Arabela A Grigorescu, Joseph HA Vissers, Dejan Ristic, Ying Z Pigli, Thomas W Lynch, Claire Wyman, Phoebe A Rice

NUCLEIC ACIDS RESEARCH | OXFORD UNIV PRESS | Published : 2009

Abstract

Rad51 is the central catalyst of homologous recombination in eukaryotes and is thus critical for maintaining genomic integrity. Recent crystal structures of filaments formed by Rad51 and the closely related archeal RadA and eubacterial RecA proteins place the ATPase site at the protomeric interface. To test the relevance of this feature, we mutated conserved residues at this interface and examined their effects on key activities of Rad51: ssDNA-stimulated ATP hydrolysis, DNA binding, polymerization on DNA substrates and catalysis of strand-exchange reactions. Our results show that the interface seen in the crystal structures is very important for nucleoprotein filament formation. H352 and R3..

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University of Melbourne Researchers

Grants

Awarded by National Institutes of Health


Awarded by NCI program project


Awarded by NATIONAL CANCER INSTITUTE


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Funding Acknowledgements

National Institutes of Health (GM058827 to P. A. R.); Susan G. Komen fellowship (to A. A. G.); Dutch Cancer Society scholarship (to J. H. A. V.); Association of International Cancer Research (to C. W.) and NCI program project (CA92584 to C. W.). Funding for open access charge: National Institutes of Health (GM058827).