In humans, the accurate pairing and segregation of homologous chromosomes during the first meiotic division is essential to the formation of viable gametes. This process requires crossing over, a conserved mechanism that results in the reciprocal exchange of chromosome arms between maternal and paternal homologs. In budding yeast, crossovers are primarily generated through the Class I crossover pathway where programmed DNA double-strand breaks are processed into double-Holliday junction intermediates that are resolved in a biased manner through the actions of the Mlh1-Mlh3 endonuclease in connection with Exo1. Despite hints that Mlh1-Mlh3 may perform additional functions in meiosis, it remains unknown what substrates and binding partners would facilitate this function. To identify interactors of Mlh3 which may provide clues pertaining to such roles, I performed a screen in budding yeast using sensitized mlh3 alleles proficient for meiotic crossover formation but defective for the DNA mismatch repair function of Mlh3. In addition to identifying previously known MLH3 interactors, I identified a novel genetic interaction with the recombinase gene DMC1 and verified that Mlh3 physically interacts with Dmc1 biochemically. Furthermore, I have shown that Mlh3 interacts with Dmc1 in vivo at a time concurrent with strand invasion. I also found that delaying expression of MLH3 to after the time when Dmc1 in thought to function resulted in mlh3∆ levels of crossing over. The above information, supported through genetic interactions between DMC1 and mlh3 separation of function mutations, suggest that Mlh1-Mlh3 is recruited to recombination intermediates early and forms a physical connection with Dmc1 which in turn stabilizes Mlh1-Mlh3 polymer formation required to generate crossovers