{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,2,6]],"date-time":"2026-02-06T10:23:04Z","timestamp":1770373384894,"version":"3.49.0"},"posted":{"date-parts":[[2026,1,23]]},"group-title":"Genetics","reference-count":99,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,1,23]],"date-time":"2026-01-23T00:00:00Z","timestamp":1769126400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,1,23]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  Mismatch repair (MMR) is a highly conserved DNA repair pathway that promotes genome stability by directing the repair of errors in DNA replication. In\n                  <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                  , MMR is initiated by either Msh2-Msh3 or Msh2-Msh6, via recognition of insertion deletion loops (IDLs; up to \u223c 17 nucleotides) and misincorporation events, respectively. Both complexes recognize and bind small (1-2 nucleotide) IDLs. Once bound, MSH complexes recruit one or more downstream MLH complexes to continue repair: Mlh1-Pms1, Mlh1-Mlh2 and\/or Mlh1-Mlh3. Msh2-Msh3 also promotes\n                  <jats:italic>CAG<\/jats:italic>\n                  trinucleotide repeat (TNR) expansions through specific DNA-binding to TNR DNA structures, followed by recruitment of MLH complexes. These expansions lead to genome instability that causes neurodegenerative diseases such as Huntington\u2019s Disease in humans. Here, we defined a hierarchy of MLH function in these Msh2-Msh3-mediated pathways\n                  <jats:italic>in vivo<\/jats:italic>\n                  in\n                  <jats:italic>S. cerevisiae<\/jats:italic>\n                  . We determined that Mlh1-Pms1 is the primary MLH complex required in Msh2-Msh3-mediated MMR. In contrast, all three MLH complexes were required to promote\n                  <jats:italic>CAG<\/jats:italic>\n                  expansions, with loss of Mlh1-Pms1 or Mlh1-Mlh2 exhibiting the strongest effects. Mutations in\n                  <jats:italic>PMS1<\/jats:italic>\n                  and\n                  <jats:italic>MLH3<\/jats:italic>\n                  were synergistic. We propose a model in which Mlh1-Pms1 is primarily responsible for \u201cappropriate\u201d Msh2-Msh3-mediated MMR, while all three MLH complexes collaborate specifically in the presence of\n                  <jats:italic>CAG<\/jats:italic>\n                  structure, to promote a \u201cpathogenic\u201d Msh2-Msh3-mediated pathway that leads to expansions. Our model highlights the importance of DNA structure-dependent conformations in modulating MLH function.\n                <\/jats:p>","DOI":"10.64898\/2026.01.20.700715","type":"posted-content","created":{"date-parts":[[2026,1,23]],"date-time":"2026-01-23T22:36:05Z","timestamp":1769207765000},"source":"Crossref","is-referenced-by-count":0,"title":["Mismatch repair MLH complexes make distinct contributions to post-replicative mismatch repair versus trinucleotide repeat expansions"],"prefix":"10.64898","author":[{"given":"Katherine M.","family":"Casazza","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY, 14203"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Greg M.","family":"Williams","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY, 14203"},{"name":"Curia Global, Inc., Buffalo, NY, 14203"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lauren","family":"Johengen","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY, 14203"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maxwell","family":"Keller","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY, 14203"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luke D.","family":"Hess","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Samantha","family":"Phelps","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natalie A.","family":"Lamb","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4243-0933","authenticated-orcid":false,"given":"Jennifer A.","family":"Surtees","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY, 14203"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"54368","reference":[{"key":"2026020503385055000_2026.01.20.700715v1.1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1006974"},{"key":"2026020503385055000_2026.01.20.700715v1.2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkad175"},{"key":"2026020503385055000_2026.01.20.700715v1.3","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(87)54076-9"},{"key":"2026020503385055000_2026.01.20.700715v1.4","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1004327"},{"key":"2026020503385055000_2026.01.20.700715v1.5","doi-asserted-by":"crossref","unstructured":"Casazza, K. 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