Abstract: Meiosis is the essential cell-division process that organizes the genetic material of one diploid parent cell into four haploid gametes, each carrying one-fourth of the genetic material in a novel assortment of genes. A key mediator of this pathway in S. cerevisiae is the Zip1 protein, which is the transverse filament protein of the synaptonemal complex (SC) which assembles along the length of homologous chromosomes during prophase I of meiosis. Some analog of the SC is conserved across all sexually-reproducing species. Zip1 is required for both SC assembly and for recombination of genetic material between homologous chromosomes, which is necessary to ensure proper disjunction of chromosomes into daughter cells. However, much remains unknown about the specific factors Zip1 interacts with to mediate these two ubiquitous pathways in meiosis. Here, Zip1 interaction with other meiotic proteins was investigated via insertion of the biotinylase enzyme TurboID at various loci along the length of the Zip1 protein. This proximity labeling technique allows identification of close-interacting partners of a protein of interest via detection of biotin ligated onto lysine residues of nearby proteins. Since previous experiments found that insertion of other tags onto the N or C terminus interfered with normal Zip1 activity, this experiment chose multiple loci along the length of the Zip1 protein for TurboID insertion in order to better identify Zip1 interactions in meiosis.
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