Characterization of the Moh1 protein in the yeast model

Date

2024-8-29

Author

Olgun, Çağla Ece

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The primary circulating estrogen hormone, 17β-estradiol (E2), plays important roles in the physiology and pathophysiology of many tissues. The regulation of cell functions in tissues in response to E2 is mediated primarily by estrogen receptor (ER) alpha, a transcription factor. Identifying E2-responsive genes and protein products could be critical for developing prognostic tools or therapeutic targets. Our previous studies revealed that YPEL2 is an estrogen-responsive gene, which is a member of a YPEL family, YPEL1- YPEL5, with highly conserved sequence homology encoding YPEL proteins with similar structural and functional features. This similarity renders deciphering the functional features of YPEL2 in the presence of other YPELs difficult. Nevertheless, using an inducible expression system we showed that YPEL2 interacts with proteins involved in oxidative stress. However, the mechanism by which YPEL2 exerts its effects is unclear. In yeast, there is one YPEL homolog: MOH1. This provides an opportunity to analyze YPEL2 functions independently of YPELs using yeast complementation approaches. Although mechanisms are unknown, my MSc studies on Moh1p functions suggested that MOH1 contributes to stress responses affecting cell survival. In this study, I aimed to attribute functions to Moh1p using the MOH1-deleted yeast strain, moh1∆, and assess its effect on cell morphology, biomolecular composition, and transcriptomic profile. Our scanning electron microscopy studies indicate structural alterations in the cell wall of moh1∆. Fourier Transform Infrared Spectroscopy and RNA sequencing reveal dramatic lipid and protein modifications resulting from differentially expressed genes that encode proteins involved in lipid and protein metabolisms and stress responses.

Subject Keywords

MOH1, S. Cerevisiae, FT-IR, RNA-Sequencing, Scanning Electron Microscopy

URI

https://hdl.handle.net/11511/111489

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Graduate School of Natural and Applied Sciences, Thesis