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Doc induces cell death by inhibiting translation; however, the mechanism of Doc-induced cell death and the cellular target of the toxin were unknown. One theory suggested that Doc inhibits translation elongation by binding directly to the 30S ribosomal subunit. Later evidence showed catalytic activity in distant homologs of Doc. These homologs contain a Fic-domain that has been shown to modify target GTPases by AMPylation and phosphocholination. Therefore, [35S] – Met, α[32P] – ATP, and γ[32P] – ATP were used in conjunction with an S30 extract to confirm that Doc inhibits translation, to assess the mechanism of modification, and to identify the modified target. The results showed that Doc is an enzyme that inhibits translation and phosphorylates a protein target.
| Advisor: | Magnuson, Roy |
| Commitee: | Cruz-Vera, Luis, MacGregor, Gordon |
| School: | The University of Alabama in Huntsville |
| Department: | Biological Sciences |
| School Location: | United States -- Alabama |
| Source: | MAI 54/02M(E), Masters Abstracts International |
| Source Type: | DISSERTATION |
| Subjects: | Molecular biology, Microbiology |
| Keywords: | Bacteriophage p1, Doc, Doc-induced phosphorylation, Fic-domain, Phd, Toxin-antitoxin system |
| Publication Number: | 1570494 |
| ISBN: | 9781321391008 |
