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. 2023 Feb 25;51(6):2725–2739. doi: 10.1093/nar/gkad096

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© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Model for MutLα activities in mismatch repair. (A) MutLα is recruited to topologically complex DNA near a mismatch (red) by a MutS homolog (shown here as MutSα). MutLα proteins form an oligomer which can associate the two daughter DNA duplexes and reposition helical crossovers that can form behind the replication fork. MutLα is activated through the DNA–DNA association and via interaction with PCNA that is either loaded near the mismatch site or left behind by the replication machinery. MutLα alters the DNA topology in the vicinity of the mismatch through facilitating interaction with two duplex regions, one actively (which it will nick) and the other passively. (B, C) Repositioning of the topological barrier allows a long tract of DNA to be available for processive components of the DNA mismatch repair process that may be inhibited by topological barriers. See Discussion for additional details.