msh2 atpase domain mutation affects ctg？cag repeat instability in transgenic micemsh2 atp酶域突变影响ctg cag重复不稳定的转基因小鼠.pdfVIP

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msh2 atpase domain mutation affects ctg？cag repeat instability in transgenic micemsh2 atp酶域突变影响ctg cag重复不稳定的转基因小鼠.pdf

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msh2 atpase domain mutation affects ctg？cag repeat instability in transgenic micemsh2 atp酶域突变影响ctg cag重复不稳定的转基因小鼠

MSH2 ATPase Domain Mutation Affects CTGNCAG Repeat Instability in Transgenic Mice ´ ´ 1 2,3 4 2,3 1 Stephanie Tome , Ian Holt , Winfried Edelmann , Glenn E. Morris , Arnold Munnich , Christopher E. 5 ` 1 Pearson , Genevieve Gourdon * ´ ˆ 1 INSERM, U781, Universite Paris Descartes, Hopital Necker-Enfants Malades, Paris, France, 2 Wolfson Centre for Inherited Neuromuscular Disease, RJAH Orthopaedic Hospital, Oswestry, Shropshire, United Kingdom, 3 Institute of Science and Technology in Medicine, Keele University, Keele, Staffordshire, United Kingdom, 4 Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York, New York, United States of America, 5 Program of Genetics and Genome Biology, The Hospital for Sick Children, Department of Molecular Genetics, University of Toronto, Toronto, Canada Abstract Myotonic dystrophy type 1 (DM1) is associated with one of the most highly unstable CTGNCAG repeat expansions. The formation of further repeat expansions in transgenic mice carrying expanded CTGNCAG tracts requires the mismatch repair (MMR) proteins MSH2 and MSH3, forming the MutSb complex. It has been proposed that binding of MutSb to CAG hairpins blocks its ATPase activity compromising hairpin repair, thereby causing expansions. This would suggest that binding, but not ATP hydrolysis, by MutSb is critical for trinucleotide expansions. However, it is unknown if the MSH2 ATPase activity is dispensible for instability. To get insight into the mechanism by which MSH2 generates trinucleotide expansions, we crossed DM1 transgenic mice carrying a highly unstable .(CTG)300 repeat tra