Date of Award

12-2006

Level of Access Assigned by Author

Campus-Only Thesis

Degree Name

Master of Science (MS)

Department

Biochemistry

Advisor

Robert E. Gundersen

Second Committee Member

John T. Singer

Third Committee Member

Robert E. Cashon

Abstract

Heterotrimeric guanine nucleotide binding proteins (G proteins) are crucial in a broad range of eukaryotic signaling pathways. They function by activating downstream effectors in response to receptor-ligand binding. In the soil amoebae Dictyostelium discoideum, the transition from unicellular to multicellular development during starvation is dependent upon G protein signaling. These G proteins require a post-translational acylation involving the attachment of palmitic acid for proper localization and function. The mechanism by which proteins are palmitoylated is still a topic of controversy. However, a group of putative palmitoyltransferases has been identified in Saccharomyces cerevisiae containing novel cysteine rich domain characterized by a four amino acid motif: DHHC. A BLAST search of the palmitoyltransferase gene from yeast identified 14 DHHC domain containing genes in D. discoideum. Characterization of phenotypic abnormalities during over-expression of the putative palmitoyltransferase genes along with computational characterization of these 14 genes will provide a foundation on which further experiments can be based.

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