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Papers In Press, published online ahead of print May 1, 2002
J. Biol. Chem, 10.1074/jbc.M202282200
Submitted on March 8, 2002
Revised on April 25, 2002
Accepted on April 30, 2002
Ludwig Institute for Cancer Research, La Jolla, CA 92093-0669
Corresponding Author: rkolodner{at}ucsd.edu
Previous studies described four dominant msh6 mutations that interfered with both the MSH2-MSH6 and MSH2-MSH3 mismatch recognition complexes (Das Gupta, R., and Kolodner, R. D. (2000) Nat. Genet. 24, 53-56). Modeling predicted that two of the amino acid substitutions (G1067D, G1142D) interfere with protein-protein interactions at the ATP binding site-associated dimer interface, one (S1036P) similarly interferes with protein-protein interactions and effects the MSH2 ATP binding site and one (H1096A) effects the MSH6 ATP binding site. The ATPase activity of the MSH2-msh6-G1067D and MSH2-msh6-G1142D complexes was inhibited by GT, +A and +AT mispairs and these complexes showed increased binding to GT and +A mispairs in the presence of ATP. The ATPase activity of the MSH2-msh6-S1036P complex was inhibited by a GT mispair and it bound the GT mispair in the presence of ATP whereas its interaction with insertion mispairs was unchanged compared to the wild-type complex. The ATPase activity of the MSH2-msh6-H1096A complex was generally attenuated and its mispair-binding behavior was uneffected. These results are in contrast to the wild-type MSH2-MSH6 complex, which showed mispair stimulated ATPase activity and ATP inhibition of mispair binding. These results indicate that the dominant msh6 mutations cause more stable binding to mispairs and suggests there may be differences in how base base and insertion mispairs are recognized.
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