Mismatch Repair |
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| Authors: | Richard Fishel |
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| Institution: | From the ‡Department of Molecular Virology, Immunology and Medical Genetics, The Ohio State University Wexner Medical Center, Columbus, Ohio 43210 and ;the §Department of Physics and the Biophysics Program, The Ohio State University, Columbus, Ohio 43210 |
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| Abstract: | Highly conserved MutS homologs (MSH) and MutL homologs (MLH/PMS) are the fundamental components of mismatch repair (MMR). After decades of debate, it appears clear that the MSH proteins initiate MMR by recognizing a mismatch and forming multiple extremely stable ATP-bound sliding clamps that diffuse without hydrolysis along the adjacent DNA. The function(s) of MLH/PMS proteins is less clear, although they too bind ATP and are targeted to MMR by MSH sliding clamps. Structural analysis combined with recent real-time single molecule and cellular imaging technologies are providing new and detailed insight into the thermal-driven motions that animate the complete MMR mechanism. |
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| Keywords: | cancer biology DNA mismatch repair DNA repair mutagenesis single-molecule biophysics hMSH2 hMLH1 hereditary non-polyposis colorectal cancer Lynch syndrome single molecule analysis |
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