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Date of Award

1-6-1997

Document Type

Restricted Thesis: Campus only access

Degree Name

Bachelor of Science

Department

Biology

First Advisor

Dr. Valerie Kish

Abstract

Ubiquitin is used by virtually all eukaryotic cells to aid in proteolysis, often for cell cycle control or cellular differentiation. Previous studies have suggested that ubiquitin is covalently bound to a protein, and recognized by the 26S protease. In order to unravel more of the mystery about the mechanism utilized by ubiquitin, a protein utilizing a ubiquitin-dependent pathway for its degradation, must be identified. The cellular differentiation of Chlamydomonas reinhardtii, from a vegetative cell to a gamete, was investigated to identify a protein that could be used as a possible tool for the study of ubiquitin. Western blot analysis shows that tubulin, a major component of the organisms flagella, is degraded during the process of gametogenesis. Western analysis also indicates a possible connection between the degradation of tubulin and the presence of ubiquitin.

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