The relationship between translocon modification and translocon quality control

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dc.contributor.advisor Rubenstein, Eric
dc.contributor.author Richards, Kyle
dc.date.accessioned 2021-08-10T18:29:28Z
dc.date.available 2021-08-10T18:29:28Z
dc.date.issued 2021-05-07
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/123456789/202743
dc.description Access to thesis permanently restricted to Ball State community only. en_US
dc.description.abstract The endoplasmic reticulum (ER) is the entry point for most proteins residing and functioning in the eukaryotic endomembrane system. The primary mechanism by which proteins enter the ER is via the translocon complex. Dysfunction in this complex can block access into the ER, which is detrimental to cellular health. Studies of translocon dysfunction in the model organism Saccharomyces cerevisiae (budding yeast) have historically relied on epitope tags to study protein interactions. I have found that a tag on the translocon pore subunit previously suggested not to impair translocon function subtly affects translocation of proteins into the ER in yeast cells. Intriguingly, this tag also suppresses a phenotype associated with defective protein quality control pathways, consistent with a functional link between translocation and quality control. I have further characterized the effects modification have on translocon quality control and cellular health, and investigated the impact of a panel of epitope tags on translocon function to identify an epitope-tagged translocon complex that functions normally for use in future experiments. en_US
dc.title The relationship between translocon modification and translocon quality control en_US
dc.description.degree Thesis (M.P.A.) en_US


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  • Master's Theses [5454]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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