hXRCC2 enhances ADP/ATP processing and strand exchange by hRAD51

doi:10.1074/jbc.M306066200

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Papers In Press, published online ahead of print May 3, 2004
J. Biol. Chem, 10.1074/jbc.M306066200
Submitted on June 9, 2003
Revised on April 29, 2004
Accepted on May 2, 2004

hXRCC2 enhances ADP/ATP processing and strand exchange by hRAD51

Kang Sup Shim, Christoph Schmutte, Gregory Tombline, and Richard Fishel

Microbiology and Immunology, Kimmel Cancer Center, Philadelphia, PA 19107

Corresponding Author: rfishel{at}lac.jci.tju.edu

The assembly of bacterial RecA, and its human homolog hRAD51, into an operational ADP/ATP-regulated DNA-protein (nucleoprotein) filament (NPF) is essential for homologous recombination repair (HRR). Yet, hRAD51 lacks the coordinated ADP/ATP processing exhibited by RecA and is less efficient in HRR reactions in vitro. Here we demonstrate that hXRCC2, one of five other poorly understood non-redundant human mitotic RecA homologs (hRAD51B, hRAD51C, hRAD51D, hXRCC2 and hXRCC3), stimulates hRAD51 ATP processing. hXRCC2 also increases hRAD51-mediated DNA unwinding and strand exchange activities that are integral for HRR. While there does not appear to be a long-lived interaction between hXRCC2 and hRAD51, we detail a strong adenosine nucleotide-regulated interaction between the hXRCC2-hRAD51D heterodimer and hRAD51. These observations begin to elucidate the separate and specialized functions of the human mitotic RecA homologs that enable an efficient NPF required for HRR.

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				C. W. Fung, G. S. Fortin, S. E. Peterson, and L. S. Symington The rad51-K191R ATPase-Defective Mutant Is Impaired for Presynaptic Filament Formation Mol. Cell. Biol., December 15, 2006; 26(24): 9544 - 9554. [Abstract] [Full Text] [PDF]

				M. Kojic, Q. Zhou, M. Lisby, and W. K. Holloman Rec2 Interplay with both Brh2 and Rad51 Balances Recombinational Repair in Ustilago maydis Mol. Cell. Biol., January 15, 2006; 26(2): 678 - 688. [Abstract] [Full Text] [PDF]

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