Submission Date
4-26-2024
Document Type
Paper- Restricted to Campus Access
Department
Biochemistry & Molecular Biology
Adviser
Rebecca Lyczak
Committee Member
Samantha Wilner
Committee Member
Stephen C. Kolwicz Jr.
Department Chair
Eric Williamsen
Department Chair
Anthony Lobo
Project Description
Puromycin-sensitive aminopeptidases (PSAs) are M1 family metalloproteases that regulate the cell cycle, fertility, and embryogenesis in many organisms. The PSA homolog found in the nematode Caenorhabditis elegans is known as PAM-1, and it cleaves the N-terminus of unknown target proteins. The PAM-1 protein is required for embryogenesis, cell cycle progression and polarization of the anteroposterior (AP) body axis. Suppressor mutations in C. elegans pam-1 mutants have been shown to significantly improve embryonic survival and restore polarity phenotypes. One novel suppressor of pam-1, spam-3(lz6), is of further interest because it has been shown to increase embryonic viability from 7.1% in pam-1(or347) mutant worms to 78.53% in pam-1(or347) mutants with the lz6 suppressor. In this study, pam-1 mutants demonstrate defects in early embryo polarity phenotypes necessary for AP axis formation that are significantly rescued in the presence of the lz6 suppressor mutation. This study further explores the mechanisms by which lz6 restores polarity by comparing the functional role and expression levels of non-muscle myosin II (NMY-II), a protein necessary for the maintaining the asymmetry in the C. elegans one-cell embryo, in pam-1 mutants and pam-1 mutants homozygous for the lz6 suppressor.
Recommended Citation
Adams, Brooke, "The Function and Expression of Non-Muscle Myosin (II) in Caenorhabditis elegans Puromycin-Sensitive Aminopeptidase (PAM-1) Mutants" (2024). Biochemistry and Molecular Biology Honors Papers. 21.
https://digitalcommons.ursinus.edu/biochem_hon/21
