Submission Date

7-23-2021

Document Type

Paper- Restricted to Campus Access

Department

Biology

Faculty Mentor

Rebecca Lyczak

Comments

Presented during the 23rd Annual Summer Fellows Symposium, July 23, 2021 at Ursinus College.

Project Description

PAM-1 is a puromycin sensitive aminopeptidase responsible for cleaving the amino acid from the N-terminus of unknown target proteins. In our model system, a microscopic nematode known as C. elegans, functional PAM-1 is required for proper polarity establishment, centrosome positioning, asymmetric division, cytoskeleton development, as well as meiosis. Due to these defects, pam-1 mutants have a reduced hatch rate to around 2%, compared to the wildtype hatch rate of 100%. A secondary suppressor of pam-1, an inhibitory kinase known as wee-1.3 involved in regulating oocyte maturation, rescues this reduced hatch rate back to around 42%. Previous research has shown that pam-1 rescues the loss of wee-1.3(RNAi) phenotype of precocious oocyte maturation. In my research, I am investigating if the suppressor mutation wee-1.3 can rescue the pam-1 meiotic defects. We compare time-lapse videos of pam-1 embryos, pam-1;wee-1.3 embryos, and wild-type embryos with GFP tagged histones in order to visual the chromosomes during meiosis. We hope to determine if wee-1.3 and pam-1 interact during meiosis to rescue the pam-1 meiotic defects, similarly to how they interact during oocyte maturation to rescue the wee-1.3 precocious oocyte maturation defects.

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