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A more recent version of this article appeared on September 5, 2003 Originally published In Press as doi:10.1074/jbc.M305513200 on June 25, 2003
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Papers In Press, published online ahead of print June 30, 2003
J. Biol. Chem, 10.1074/jbc.M305513200
Submitted on May 27, 2003
Revised on June 30, 2003
Accepted on June 25, 2003

Assembly and molecular activities of the MutS tetramer

Keith P. Bjornson, Leonard J. Blackwell, Harvey Sage, Celia Baitinger, Dwayne Allen, and Paul Modrich

Biochemistry and HHMI, Duke Univ. Medical Center, Durham, NC 27710

Corresponding Author: modrich{at}biochem.duke.edu

Analytical equilibrium ultracentrifugation indicates that Escherichia coli MutS exists as an equilibrating mixture of dimers and tetramers. The association constant for the dimer to tetramer transition is 2.1x107 M-1, indicating that the protein would consist of both dimers and tetramers at physiological concentrations. The carboxyl terminus of MutS is required for tetramer assembly because a previously described 53 amino acid carboxyl terminal truncation(MutS800) forms a limiting species of a dimer (Obmolova et al. (2000) Nature 407, 703-710;Lamers et al. (2000) Nature 407, 711-717). MutS800 binds a 20 base pair heteroduplex an order of magnitude more weakly than full length MutS, and at saturating protein concentrations, the heteroduplex-bound mass observed with MutS800 is only half that observed with the full length protein, indicating that the subunit copy number of heteroduplex-bound MutS is twice that of MutS800. Analytical equilibrium ultracentrifugation using a fluorescein-tagged 20 base pair heteroduplex demonstrated that native MutS forms a tetramer on this single site size heteroduplex DNA. Equilibrium fluorescence experiments indicated that dimer to tetramer assembly promotes mismatch binding by MutS and that the tetramer can bind only a single heteroduplex molecule, implying nonequivalence of the two dimers within the tetramer. As compared to native MutS, the ability of MutS800 to promote MutL-dependent activation of MutH is substantially reduced.


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