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Investigating the Role of a Charge-Charge Interface in Chromosome Pairing

Year: 2023

Presenter Name: Jesus Aguayo

Meiosis is a specialized cell division process whereby gametes arise in preparation for fertilization. Exploring the meiotic process has shed light on mankind's understanding of the natural biological processes from reproduction to genetic engineering. The Synaptonemal Complex is a structure that forms during meiosis. This structure orients and aligns the two parental chromosomes which then allows for genetic exchange between them. Once germ cells have undergone meiosis, they are ready for the fertilization process which then results in offspring in ideal circumstances. Additionally, the SC allows for a precise number of gene exchanges between each set of chromosomes. Without the SC, there would be errors in the sets of chromosomes in a cell, reduced number of offspring, infertility, and more.
The SC is a highly conserved structure that is found in simple sexual reproducing organisms as well as complex multicellular organisms such as humans. If the SC were better understood, the quality of life of humans could be improved. Whether it's helping an infertile individual receive treatment to be able to reproduce or to better understand conditions that result from aneuploidy in humans and other creatures, it's undeniable that researching the SC is worthwhile.
Using CRISPR/Cas9 technology, progeny and male count methods, immunofluorescent staining, and confocal imaging, I was able to obtain insights as to how the SC functions within the nematode Caenorhabditis elegans. Specifically, I focused on conditions that suppress a temperature sensitive mutation, syp-1 K42E.
The data from progeny counts indicates that mutating certain specific proteins within the SC (syp-3 D62V, syp-3 D62N, and syp-4 E90K) can suppress the temperature sensitive mutation when they are each found in the same SC structure as the syp-1 K42E strain but they are unable to significantly cause any change when the temperature sensitive mutation is not present in the same structure. Immunofluorescent imaging also indicated that there was no significant difference between the suppressor strains and the wildtype strain.
The findings from testing the individual strains without the suppressor strain gave insight as to the importance of charged interactions between the proteins within the SC. Since Lysine (K) was replaced by Glutamic acid (E) in the SYP-1 K42E protein, there was a significant difference between the wildtype C. elegans strain and the syp-1 K42E strain. However, the suppressor proteins were able to restore the phenotype of the C. elegans that had both the suppressor protein and the SYP-1 K42E protein.
University / Institution: University of Utah
Type: Poster
Format: In Person
Presentation #D61
SESSION D (3:30-5:00PM)
Area of Research: Science & Technology
Faculty Mentor: Ofer Rog