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J. Biol. Chem., Vol. 277, Issue 28, 25545-25553, July 12, 2002
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, and
From the Ludwig Institute for Cancer Research, Cancer Center, and
Department of Medicine, University of California San Diego School
of Medicine, La Jolla, California 92093-0660
A previous study described four dominant
msh6 mutations that interfere 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 and G1142D)
interfere with protein-protein interactions at the ATP-binding
site-associated dimer interface, one (S1036P) similarly interferes with
protein-protein interactions and affects the Msh2 ATP-binding site, and
one (H1096A) affects 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 with the wild-type
complex. The ATPase activity of the Msh2-Msh6-H1096A complex was
generally attenuated, and its mispair-binding behavior was unaffected.
These results are in contrast to those obtained with 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 suggest that there may be differences in how base
base and insertion mispairs are recognized.
Present address: engeneOS, 40 Bear Hill Rd., Waltham, MA 02451.
§
To whom correspondence should be addressed: Ludwig Inst. for Cancer
Research, University of California San Diego School of Medicine, CMME
3080, 9500 Gilman Dr., La Jolla, CA 92093-0669. Tel.: 858-534-7804;
Fax: 858-534-7750; E-mail: rkolodner@ucsd.edu.
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