(full paper is archived in the Miller Library)
Title: The cloning and sequencing of UBCT1, the Tigriopus californicus homologue of the yeast UBC4 and UBC5 gene
Student Author(s): Lee, Daniel S.
Faculty Advisor(s): Levine, R. Paul.
Location: Final Papers Biology 175H
Date: June 1993
Abstract: Ubiquitin is a small protein-binding protein that is found in all eukaryotes. It displays a high degree of conservation among organisms. It is involved in many cellular functions including DNA repair, cell cycle control, and the stress response. There are several classes of ubiquitin-protein ligating enzymes that are involved in the ubiquitin system, the ubiquitin-conjugating enzymes (UBC's), confer specificity to the ubiquitin by selecting which proteins to tag with ubiquitin. In the yeast, Saccharomyces cerevisiae, 2 UBC's have been shown to be induced by heat shock and are involved in the stress response. Tigriopus californicus, a copepod abundant in the high splash pools of the California Coast, displays an ability to tolerate wide environmental fluctuations in temperature and salinity. DNA and RNA were succesfully isolated from T. californicus. Three genes coding for ubiquitin were found. One ubiquitin-conjugating enzyme gene was found and sequenced (UBCT1). The homology between the UBCT1 gene and yeast UBC4 and UBC5 is extremely high, indicating that UBCT1 expression may also be induced during heat shock and play a role in the stress response.