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M109917200v1
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Papers In Press, published online ahead of print February 11, 2002
J. Biol. Chem, 10.1074/jbc.M109917200
Submitted on October 12, 2001
Revised on February 7, 2002
Accepted on February 10, 2002

Biochemical characterization of the human RAD51 Protein: III. Modulation of DNA binding by adenosine nucleotides

Christopher D Heinen, Gregory Tombline, Kang-Sup Shim, and Richard Fishel

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

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

Adenosine nucleotides affect the ability of RecA•ssDNA1 nucleoprotein filaments to cooperatively assume and maintain an extended structure that facilitates DNA pairing during recombination. Here we have determined that ADP and ATP/ATPgS affect the DNA binding and aggregation properties of the human RecA homolog hRAD51. These studies have revealed significant differences between hRAD51 and RecA. In the presence of ATPgS, RecA forms a stable complex with ssDNA, while the hRAD51 ssDNA complex is destabilized. Conversely in the presence of ADP and ATP, the RecA ssDNA complex is unstable, while the hRAD51 ssDNA complex is stabilized. We identified two hRAD51•ssDNA binding forms by gel shift analysis, which were distinct from a well-defined RecA•ssDNA binding form. The available evidence suggests that a low molecular weight hRAD51•ssDNA binding form (hRAD51•ssDNAlow) correlates with active exchange of ADP for ATP. A high molecular weight hRAD51•ssDNA aggregate (hRAD51•ssDNAhigh) appears to correlate with a form that fails to exchange ADP for ATP. Our data are consistent with the notion that hRAD51 is unable to appropriately coordinate ssDNA binding with adenosine nucleotide processing. These observations suggest that other factors may assist hRAD51 in order to mirror RecA recombinational function.


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