Dynamic DNA binding licenses a repair factor to bypass roadblocks in search of DNA lesions

Maxwell W. Brown, Yoori Kim, Gregory M. Williams, John D. Huck, Jennifer A. Surtees and Ilya J. Finkelstein ()
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Maxwell W. Brown: Institute for Cellular and Molecular Biology, The University of Texas at Austin
Yoori Kim: Institute for Cellular and Molecular Biology, The University of Texas at Austin
Gregory M. Williams: School of Medicine and Biomedical Sciences, State University of New York at Buffalo
John D. Huck: School of Medicine and Biomedical Sciences, State University of New York at Buffalo
Jennifer A. Surtees: School of Medicine and Biomedical Sciences, State University of New York at Buffalo
Ilya J. Finkelstein: Institute for Cellular and Molecular Biology, The University of Texas at Austin

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract DNA-binding proteins search for specific targets via facilitated diffusion along a crowded genome. However, little is known about how crowded DNA modulates facilitated diffusion and target recognition. Here we use DNA curtains and single-molecule fluorescence imaging to investigate how Msh2–Msh3, a eukaryotic mismatch repair complex, navigates on crowded DNA. Msh2–Msh3 hops over nucleosomes and other protein roadblocks, but maintains sufficient contact with DNA to recognize a single lesion. In contrast, Msh2–Msh6 slides without hopping and is largely blocked by protein roadblocks. Remarkably, the Msh3-specific mispair-binding domain (MBD) licences a chimeric Msh2–Msh6(3MBD) to bypass nucleosomes. Our studies contrast how Msh2–Msh3 and Msh2–Msh6 navigate on a crowded genome and suggest how Msh2–Msh3 locates DNA lesions outside of replication-coupled repair. These results also provide insights into how DNA repair factors search for DNA lesions in the context of chromatin.

Date: 2016
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DOI: 10.1038/ncomms10607

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