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- Title
MutS switches between two fundamentally distinct clamps during mismatch repair.
- Authors
Jeong, Cherlhyun; Cho, Won-Ki; Song, Kyung-Mi; Cook, Christopher; Yoon, Tae-Young; Ban, Changill; Fishel, Richard; Lee, Jong-Bong
- Abstract
Single-molecule trajectory analysis has suggested DNA repair proteins may carry out a one-dimensional (1D) search on naked DNA encompassing >10,000 nucleotides. Organized cellular DNA (chromatin) presents substantial barriers to such lengthy searches. Using dynamic single-molecule fluorescence resonance energy transfer, we determined that the mismatch repair (MMR) initiation protein MutS forms a transient clamp that scans duplex DNA for mismatched nucleotides by 1D diffusion for 1 s (~700 base pairs) while in continuous rotational contact with the DNA. Mismatch identification provokes ATP binding (3 s) that induces distinctly different MutS sliding clamps with unusual stability on DNA (~600 s), which may be released by adjacent single-stranded DNA (ssDNA). These observations suggest that ATP transforms short-lived MutS lesion scanning clamps into highly stable MMR signaling clamps that are capable of competing with chromatin and recruiting MMR machinery, yet are recycled by ssDNA excision tracts.
- Subjects
DNA repair; DNA; CHROMATIN; NUCLEOTIDES; BIOCHEMICAL genetics; ADENOSINE triphosphate
- Publication
Nature Structural & Molecular Biology, 2011, Vol 18, Issue 3, p379
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2009