JBC Invitrogen Ultrasensitive Cytokine Assays

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Originally published In Press as doi:10.1074/jbc.M104256200 on July 13, 2001

J. Biol. Chem., Vol. 276, Issue 36, 34339-34347, September 7, 2001
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Distinct MutS DNA-binding Modes That Are Differentially Modulated by ATP Binding and Hydrolysis*

Leonard J. Blackwell, Keith P. Bjornson, Dwayne J. AllenDagger , and Paul Modrich§

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

The role of MutS ATPase in mismatch repair is controversial. To clarify further the function of this activity, we have examined adenine nucleotide effects on interactions of Escherichia coli MutS with homoduplex and heteroduplex DNAs. In contrast to previous results with human MutSalpha , we find that a physical block at one end of a linear heteroduplex is sufficient to support stable MutS complex formation in the presence of ATP·Mg2+. Surface plasmon resonance analysis at low ionic strength indicates that the lifetime of MutS complexes with heteroduplex DNA depends on the nature of the nucleotide present when MutS binds. Whereas complexes prepared in the absence of nucleotide or in the presence of ADP undergo rapid dissociation upon challenge with ATP·Mg2+, complexes produced in the presence of ATP·Mg2+, adenosine 5'-(beta ,gamma -imino)triphosphate (AMPPNP)·Mg2+, or ATP (no Mg2+) are resistant to dissociation upon ATP challenge. AMPPNP·Mg2+ and ATP (no Mg2+) reduce MutS affinity for heteroduplex but have little effect on homoduplex affinity, resulting in abolition of specificity for mispaired DNA at physiological salt concentrations. Conversely, the highest mismatch specificity is observed in the absence of nucleotide or in the presence of ADP. ADP has only a limited effect on heteroduplex affinity but reduces MutS affinity for homoduplex DNA.

* This work was supported by NIGMS Grant GM23719 from the 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.

Dagger Present address: Xanthon, P. O. Box 12296, Research Triangle Park, NC 27709.

Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 919-684-2775; Fax: 919-681-7874; E-mail: modrich@biochem.duke.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.