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J Biol Chem, Vol. 273, Issue 15, 9197-9201, April 10, 1998
From the Department of Biochemistry and ¶ Howard Hughes
Medical Institute, Duke University Medical Center, Durham,
North Carolina 27710
MutS, MutL, and DNA helicase II are required for
the mismatch-provoked excision step that occurs during
Escherichia coli methyl-directed mismatch repair. In this
study MutL is shown to enhance the unwinding activity of DNA helicase
II more than 10-fold on a conventional helicase substrate in which a
35-residue oligonucleotide is annealed to a M13 circular
single-stranded phage DNA under conditions where the two proteins are
present at approximately molar stoichiometry with respect to the
substrate. MutS- and MutL-dependent activation of DNA
helicase II has also been demonstrated with a model substrate in which
a 138-residue oligonucleotide was hybridized to a 138-nucleotide gap in
an otherwise duplex 7,100-base pair circular DNA. Displacement of the
oligonucleotide requires MutS, MutL, DNA helicase II, and ATP and is
dependent on the presence of a mismatch within the hybrid region.
Although DNA helicase II and Rep helicase share substantial sequence
homology and features of mechanism, Rep helicase is inactive in this
reaction.
MutS and MutL Activate DNA Helicase II in a
Mismatch-dependent Manner
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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