Abstract：
:Mismatch repair (MMR) is initiated by MutS family proteins (MSH) that recognize DNA mismatches and recruit downstream repair factors. We used a single-molecule DNA-unzipping assay to probe interactions between S. cerevisiae MSH2-MSH6 and a variety of DNA mismatch substrates. This work revealed a high-specificity binding state of MSH proteins for mismatch DNA that was not observed in bulk assays and allowed us to measure the affinity of MSH2-MSH6 for mismatch DNA as well as its footprint on DNA surrounding the mismatch site. Unzipping analysis with mismatch substrates containing an end blocked by lac repressor allowed us to identify MSH proteins present on DNA between the mismatch and the block, presumably in an ATP-dependent sliding clamp mode. These studies provide a high-resolution approach to study MSH interactions with DNA mismatches and supply evidence to support and refute different models proposed for initiation steps in MMR.
journal_name
Mol Celljournal_title
Molecular cellauthors
Jiang J,Bai L,Surtees JA,Gemici Z,Wang MD,Alani Edoi
10.1016/j.molcel.2005.10.014subject
Has Abstractpub_date
2005-12-09 00:00:00pages
771-81issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(05)01684-9journal_volume
20pub_type
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