Date Thesis Awarded
5-2024
Access Type
Honors Thesis -- Access Restricted On-Campus Only
Degree Name
Bachelors of Science (BS)
Department
Biology
Advisor
Diane C. Shakes
Committee Members
Shantá D. Hinton
Deborah Bebout
Abstract
C. elegans sperm employ an MSP (major sperm protein) polymerization-based sperm motility system, similar to other members of the Nematoda phylum, including well-known parasitic roundworms. Deletion of a newly characterized member of the protein tyrosine phosphatase PTP-3B superfamily, presumed pseudophosphatase SPE-54, has been shown to disrupt MSP-based treadmilling and spematozoon morphology. These defects inhibit the ability of male sperm to properly fertilize oocytes. This study demonstrates that the overall SPE-54 sequence and the altered residues of the catalytic domain are strongly conserved within Caenorhabditis and Nematoda, implying biological activity through conservation. Phosphatase activity assays conducted with recombinant SPE-54 protein expressed in HEK293 cells demonstrate no phosphatase activity even when the catalytic domain is restored to the canonical sequence, supporting alignments which suggest SPE-54 is a catalytically inactive phosphatase.
Recommended Citation
Howell, Jack, "Assessing the Catalytic Activity and Conservation of the C. elegans protein SPE-54" (2024). Undergraduate Honors Theses. William & Mary. Paper 2093.
https://scholarworks.wm.edu/honorstheses/2093
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