Date of Award

2023

Publication Type

Thesis

Degree Name

M.A.Sc.

Department

Chemistry and Biochemistry

Keywords

RNA helicase, Toxoplasma gondii, Cellular stress, Apicomplexan parasites

Supervisor

S.Ananvoranich

Supervisor

A.Hubberstey

Rights

info:eu-repo/semantics/openAccess

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Abstract

Toxoplasma gondii, an obligate intracellular apicomplexan parasite, is the causative agent of toxoplasmosis which has serious complications in immunocompromised individuals and in offspring of infected mothers. Central to the parasite’s pathogenesis and transmission is its adaptation to various forms of cellular stress. A conserved stress response by Toxoplasma gondii is translational control induced by phosphorylation of TgIF2α, during which non-translating mRNAs accumulate in messenger ribonucleoprotein (mRNP) granules that disassemble upon stress relief. DEAD-box RNA helicases are candidates involved in the regulation of mRNP granules and also function in translational control. In this study, it was shown that the flanking extensions of HoDI, a DEAD-box RNA helicase in Toxoplasma gondii, are predicted to be disordered. Compared to the extensions of its ortholog Dhh1 in S. cerevisiae, the N-terminal, and C-terminal extensions of HoDI were predicted to be more disordered and less disordered, respectively. Additionally, it was hypothesized that HoDI functions in translational repression similar to Dhh1. By designing and performing an RNA-protein tethering assay, it was shown that HoDI’s function in translational repression could not be observed to a very significant effect potentially due to the position of the MS2 coat protein used to tether HoDI to the reporter.

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