Nucleic Acids Research, Vol 27, Issue 11 2325-2331, Copyright © 1999 by Oxford University Press
L Galio, C Bouquet and P Brooks
Functional interactions of Escherichia coli MutS and MutL in mismatch
repair are dependent on ATP. In this study, we show that MutS and MutL
associate with immobilised DNA in a manner dependent on ATP hydrolysis and
with an ATP concentration near the solution K m of the ATPase of MutS.
After removal of MutS, MutL and ATP, much of the protein in this ternary
complex is not stably associated, with MutL leaving the complex more
rapidly than MutS. The rapid dissociation reveals a dynamic interaction
with concurrent rapid association and dissociation of proteins from the
DNA. Analysis by surface plasmon resonance showed that the DNA interacting
with dynamically bound protein was more resistant to nuclease digestion
than the DNA in MutS-DNA complexes. Non- hydrolysable analogs of ATP
inhibit the formation of this dynamic complex, but permit formation of a
second type of ternary complex with MutS and MutL stably bound to the
immobilised DNA.
ARTICLES
ATP hydrolysis-dependent formation of a dynamic ternary nucleoprotein complex with MutS and MutL
Genoscope, Centre National de Sequencage, BP 191, 2 rue Gaston Cremieux, 91006 Evry, France.
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