Interactions of the adenovirus E1B-55kD and E4-34kD proteins reveal a novel property of the E1B-55kD protein / by Milissa D. Johnson.
| Author/creator | Johnson, Milissa D. author. |
| Other author | Ornelles, David A., degree supervisor. |
| Other author | East Carolina University. Department of Biology. |
| Format | Theses and dissertations |
| Production | 1995. |
| Description | 95 leaves, 20 unnumbered leaves of plates : illustrations ; 28 cm |
| Supplemental Content | Access via ScholarShip |
| Subjects |
| Variant title | Abstract title: Interaction of the adenovirus E1B-55kD and E4-34kD proteins reveal a novel property of the E1B-55kD protein |
| Summary | In adenovirus-infected cells, the ElB-55kD protein complexes with the E4-34kD protein and mediates transport of mRNA from the nucleus to the cytoplasm. The work in this thesis studied the interaction of the ElB protein and the E4 protein using a series of well-characterized ElB mutant viruses. ElB genes were isolated from eleven mutant ElB viruses, cloned into an appropriate expression vector, and transfected into HeLa cells either alone or with a construct that expresses the wild-type E4 protein. The localization of the proteins was determined by indirect immunofluorescence microscopy. The wild-type ElB protein localized predominantly in the cytoplasm. When co expressed with the E4 protein, the ElB protein was found primarily in the nucleus. The wild-type E4 protein was found mostly in the nucleus whether expressed alone or co expressed with the wild-type ElB protein. The mutant ElB proteins displayed a variety of localization patterns whether expressed alone or co-expressed with the E4 protein. Seven of the mutant ElB proteins partitioned into the nucleus in the absence of the E4 protein. Furthermore, four of the mutant ElB proteins forced a portion of the E4 protein to be cytoplasmic. A correlation exists between the number of properties of the ElB mutant viruses adversely affected by the mutation and the intracellular localization of the ElB protein. Mutant viruses that display a greater number of defective properties also express an ElB protein that localizes to the nucleus to a greater extent in the absence of other viral proteins. These results suggest that the ElB-55kD protein has an inherent cytoplasmic retention property. This novel property can be disrupted by mutations that also disrupt the function of the protein during an adenovirus infection. For the wild-type ElB protein, cytoplasmic retention is relieved by interaction with the E4 protein in the cytoplasm. |
| General note | Submitted to the faculty of the Department of Biology. |
| General note | Advisor: David A. Ornelles |
| Dissertation note | M.S. East Carolina University 1995 |
| Bibliography note | Includes bibliographical references (leaves 92-95). |
| Genre/form | Academic theses. |
| Genre/form | Academic theses. |
| Genre/form | Thèses et écrits académiques. |
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