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MutS and MutL Activate DNA Helicase II in a Mismatch-dependent Manner

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Yamaguchi, Miyuki, Dao, Vivian, Modrich, Paul·1998·Journal of Biological Chemistry

Abstract

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.

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Metadata

Authors
Yamaguchi, M., Dao, V., & Modrich, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-04
Volume
273
Issue
15
Pages
9197-9201
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2083688697
Cited by
162
References
0
FWCI
3.83
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: MutS and MutL Activate DNA Helicase II in a Mismatch-dependent Manner. https://app.cochat.ai/papers/10.1074/jbc.273.15.9197
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Yamaguchi, M., Dao, V., & Modrich, P. (1998). MutS and MutL Activate DNA Helicase II in a Mismatch-dependent Manner. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.15.9197

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