Yippee-like protein Moh1 links gene expression to metabolism and selective stress resistance in Saccharomyces cerevisiae
Authors:Çağla Ece Olgun1,a, Gizem Turan Duman1,a, Gizem Güpür1, Hamit İzgi1, Mariam Huda2, Demet Çetin3, Zekiye Suludere4, Fatma Küçük Baloğlu5, Ayşe Koca Çaydaşı2 and Mesut Muyan1
doi: 10.15698/mic2026.06.881
Volume 13, pp. 261 to 280, published 29/06/2026.
1 Department of Biological Sciences, Middle East Technical University, 06800, Çankaya-Ankara, Türkiye. 2 Department of Molecular Biology and Genetics, Koç University, Istanbul, Türkiye. 3 Department of Mathematics and Science Education, Gazi Faculty of Education, Gazi University, 06500, Ankara, Türkiye. 4 Department of Biology, Faculty of Science, Gazi University, 06500, Ankara, Türkiye. 5 Department of Biology, Giresun University, Giresun, Türkiye.
Keywords:
MOH1, S. cerevisiae, stress response, SEM, RNA-Seq, FTIR
Corresponding Author(s):
Conflict of interest statement:
The authors declare no conflict of interest.
Please cite this article as:
Çağla Ece Olgun, Gizem Turan Duman, Gizem Güpür, Hamit İzgi, Mariam Huda, Demet Çetin, Zekiye Suludere, Fatma Küçük Baloğlu, Ayşe Koca Çaydaşı, Mesut Muyan (2026). Yippee-like protein Moh1 links gene expression to metabolism and selective stress resistance in Saccharomyces cerevisiae. Microbial Cell 13: 261-281. doi: 10.15698/mic2026.06.881
© 2026 Olgun et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
The Yippee-like (YPEL) proteins are a evolutionarily conserved eukaryotic family implicated in proliferation, senescence, and stress adaptation, yet their molecular functions remain poorly defined. Humans possess five paralogs (YPEL1–YPEL5), while the budding yeast S. cerevisiae contains a single ortholog, MOH1, previously linked to stress responses but with an unclear cellular role. Here, we investigated the function of MOH1 in S. cerevisiae. MOH1 deletion resulted in stressspecific phenotypes, including increased sensitivity to sodium azide and sulfuric acid, but enhanced resistance to hydrogen peroxide and acetic acid. Moh1 protein levels were dynamically regulated, decreasing upon hydrogen peroxide treatment and increasing in response to sulfuric acid. Morphological analyses including SEM revealed that moh1∆ cells are rounder, form aggregates, and exhibit altered surface architecture independently of stress. RNA profiling and FTIR spectroscopy uncovered transcriptional reprogramming and metabolic remodeling, including alterations in lipid, protein, and cell wall polysaccharide levels and composition. Functional analyses showed that increased resistance to hydrogen peroxide is not due to altered mitochondrial ROS production but rather to reduced intracellular ROS accumulation. This effect is attributed to decreased cellular uptake resulting from altered permeability, supported by resistance to Congo red and sensitivity to SDS, consistent with cell envelope remodeling. Collectively, our findings identify Moh1 as a regulatory factor linking gene expression to metabolism and cellular architecture, thereby influencing cell envelope permeability and conferring selective stress resistance in S. cerevisiae.