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Assessing the Catalytic Activity and Conservation of the C. elegans protein SPE-54
Howell, Jack
Howell, Jack
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.
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2024-05-01
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2027-05-03
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Biology