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Originally published In Press as doi:10.1074/jbc.M106120200 on November 20, 2001

J. Biol. Chem., Vol. 277, Issue 5, 3673-3679, February 1, 2002
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Differential ATP Binding and Intrinsic ATP Hydrolysis by Amino-terminal Domains of the Yeast Mlh1 and Pms1 Proteins*

Mark C. HallDagger , Polina V. ShcherbakovaDagger , and Thomas A. KunkelDagger §

From the Dagger  Laboratory of Molecular Genetics, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709

MutL homologs belong to a family of proteins that share a conserved ATP binding site. We demonstrate that amino-terminal domains of the yeast MutL homologs Mlh1 and Pms1 required for DNA mismatch repair both possess independent, intrinsic ATPase activities. Amino acid substitutions in the conserved ATP binding sites concomitantly reduce ATP binding, ATP hydrolysis, and DNA mismatch repair in vivo. The ATPase activities are weak, consistent with the hypothesis that ATP binding is primarily responsible for modulating interactions with other MMR components. Three approaches, ATP hydrolysis assays, limited proteolysis protection, and equilibrium dialysis, provide evidence that the amino-terminal domain of Mlh1 binds ATP with >10-fold higher affinity than does the amino-terminal domain of Pms1. This is consistent with a model wherein ATP may first bind to Mlh1, resulting in events that permit ATP binding to Pms1 and later steps in DNA mismatch repair.

* 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.

§ To whom correspondence should be addressed: Laboratory of Structural Biology, NIEHS, NIH, 111 T. W. Alexander Dr., Research Triangle Park, NC 27709. Tel.: 919-541-2644; Fax: 919-541-7613; E-mail: kunkel@niehs.nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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