Regulation of eucaryotic protein synthesis was studied by three different approaches. One of these studies focused on the regulation of mRNA translation in poliovirus infected cells. Evidence indicated that proteolysis of the p220 component of the CBP complex was not sufficient to obtain complete inhibition of host cell protein synthesis after poliovirus infection. This suggested the existence of an additional viral function in order to achieve the full inhibition of cellular mRNA translation observed after infection. / The effect of viral infection on host protein synthesis and, in particular, on mRNA association with the cytoskeleton was also investigated. Results indicated that (1) all mRNAs studied, appeared to associate with the cytoskeleton fraction during protein synthesis, irrespective of their 5$ sp prime$ and 3$ sp prime$ terminal structures; (2) although the association of mRNA with the cytoskeletal framework appears to be required, it was not found to be sufficient for protein synthesis to occur; (3) the shut-off of host protein synthesis during poliovirus but not vesicular stomatitis virus infection correlated with the release of host mRNAs from the cytoskeleton. / Finally, the regulation of protein synthesis during mitosis was studied. The addition of CBP complex to cell-free extracts was shown to stimulate endogenous mRNA translation in mitotic but not interphase extracts. It was found that the 24k-CBP from mitotic cells was considerably less phosphorylated than the interphase 24k-CBP. Moreover, its ability to recognize the cap structure of mRNA, as judged by cross-linking assays, was decreased in mitotic extracts. Evidence indicated that the extent of phosphorylation of the 24k-CBP did not directly affect its cap binding activity. Possible mechanisms for the regulation of the 24k-CBP activity during mitosis have been suggested.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.75350 |
| Date | January 1986 |
| Creators | Bonneau, Anne-Marie. |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Doctor of Philosophy (Department of Biochemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 000420047, proquestno: AAINL38201, Theses scanned by UMI/ProQuest. |
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