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Originally published In Press as doi:10.1074/jbc.M301101200 on March 6, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18557-18562, May 16, 2003
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Differential and Simultaneous Adenosine Di- and Triphosphate Binding by MutS*

Keith P. Bjornson and Paul ModrichDagger §

From the Department of Biochemistry and Dagger  Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710

The roles of ATP binding and hydrolysis in the function of MutS in mismatch repair are poorly understood. As one means of addressing this question, we have determined the affinities and number of adenosine di- and triphosphate binding sites within MutS. Nitrocellulose filter binding assay and equilibrium fluorescence anisotropy measurements have demonstrated that MutS has one high affinity binding site for ADP and one high affinity site for nonhydrolyzable ATP analogues per dimer equivalent. Low concentrations of 5'-adenylylimidodiphosphate (AMPPNP) promote ADP binding and a large excess of AMPPNP is required to displace ADP from the protein. Fluorescence energy transfer and filter binding assays indicate that ADP and nonhydrolyzable ATP analogues can bind simultaneously to adjacent subunits within the MutS oligomer with affinities in the low micromolar range. These findings suggest that the protein exists primarily as the ATP·MutS·ADP ternary complex in solution and that this may be the form of the protein that is involved in DNA encounters in vivo.

* This work was supported in part by Grant GM23719 from the NIGMS, National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed: Howard Hughes Medical Institute, Box 3711, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-2775; Fax: 919-681-7874; E-mail: modrich@biochem.duke.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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