image: Figure 1. Ectopically expressed EGFP-LMNA and EGFP-Progerin are targeted to the nuclear membranes of yeast cells with EGFP-Progerin disrupting cell growth, decreasing chronological lifespan and increasing genome instability. pYES vectors containing galactose inducible promoters and encoding either EGFP, EGFP-LMNA or EGFP-Progerin were transformed into BY4741 yeast and expression induced in galactose containing media. (A) 3 colony transformants were selected from plates and grown in liquid media overnight, with proteins isolated for Western blotting for EGFP. Total protein (top panels - stained with trichloroethanol (TCE)) was used for loading controls, followed by Western blotting for EGFP (bottom panel – EGFP antibody). EGFP proteins were separated on 8% SDS-PAGE gels, while proteins for EGFP-LMNA and EGFP-Progerin are separated on 12% gels. The EGFP-LMNA and EGFP-Progerin lanes were cropped from the same gel. (B) The triplicate western bands for EGFP-LMNA and EGFP-Progerin were scanned and quantified. Values are presented as mean ± SD for n=3 and were analyzed with an ordinary one-way ANOVA with post hoc Tukey's multiple comparisons test where p-value < 0.01**, p-value < 0.001***, and p-value < 0.0001****. (C) Cultures of yeast expressing EGFP (black), EGFP-LMNA (red) or EGFP-Progerin (blue) were grown in 2% Raffinose/0.2% Galactose supplemented liquid media (n = 3) with OD600 readings collected at the times shown. Log normalized OD readings were plotted for the time points. Error bars represent standard error of the mean. * represents p-values < 0.05 via 2 tailed t-test. The OD600 at 4, 8, 12 and 24 hours were plotted for growth curves conducted in 2% RAF/0.2% GAL, as shown in Supplementary Figure 1. (D) Chronological lifespan assays were conducted using methylene blue on yeast expressing EGFP (black), EGFP-LMNA (red) and EGFP-Progerin (blue) and the percent cell survival over 7 days plotted. n=3. * represents 2-tailed t-test p-value < 0.05. Comparable CLS experiments performed using the standard colony counting method are shown in Supplementary Figure 2 (n=3). (E) Colony reversion assays were performed by expressing EGFP, EGFP-LMNA or EGFP-Progerin into the YPH500 strain carrying a point mutation in the ADE2 gene. Westerns confirming correct expression of the proteins is shown in Supplementary Figure 3. This leads to yeast producing red coloration on YPD media. Red and white colonies were counted and the percentage of white colonies from EGFP (black), EGFP-LMNA (red) and EGFP-Progerin (blue) yeast was determined. The percentage of white colonies (y-axis) were scored over each day (x-axis) of the assay. Error bars - standard error of the mean (n=3). * represents p-value < 0.05, and ** via 2 tailed t-test.
Credit: Copyright: © 2026 Belak et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
“The budding yeast, Saccharomyces cerevisiae, is an excellent model for studying mechanisms governing aging, with many genetic and biochemical pathways highly conserved.”
BUFFALO, NY — April 17, 2026 — A new research paper was published in Volume 18 of Aging-US on April 3, 2026, titled “Modeling premature aging in yeast via the expression of Progerin.”
The study was led by first author Zachery R. Belak from the University of Saskatchewan, and corresponding author Troy A.A. Harkness from the University of Saskatchewan and the University of Alberta. The team developed a yeast-based model to study premature aging by expressing Progerin, the toxic protein responsible for Hutchinson–Gilford Progeria Syndrome. Using genetically engineered yeast cells, they compared the effects of Progerin with its normal counterpart, Lamin A, to better understand how protein accumulation impacts cellular aging.
Their findings show that Progerin expression leads to slower cell growth, increased genome instability, and a significant reduction in chronological lifespan. In contrast, Lamin A did not produce the same harmful effects, highlighting the specific role of Progerin in driving premature aging phenotypes.
The study also demonstrates that Progerin accumulates in aging mother cells and remains more stable than Lamin A, suggesting a mechanism by which damaged or toxic proteins are retained during the aging process. These observations mirror what has been reported in human cells, reinforcing the relevance of this model system.
“Taken together, expression of Progerin in yeast cells mimics what is observed in human cells, establishing yeast as a powerful model to discover genetic mechanisms driving premature and normal aging.”
Overall, the researchers present a practical and efficient model for studying the biological mechanisms underlying premature aging. Their work provides a valuable platform for testing new strategies aimed at reducing toxic protein accumulation and improving cellular health during aging.
Paper DOI: https://doi.org/10.18632/aging.206367
Corresponding author: Troy AA. Harkness – taharkne@ualberta.ca
Keywords: aging, Hutchinson-Gilford Progeria Syndrome, yeast, Progerin, Lamin A, premature aging
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Journal
Aging-US
Method of Research
News article
Subject of Research
Not applicable
Article Title
Modeling premature aging in yeast via the expression of Progerin
Article Publication Date
3-Apr-2026
COI Statement
The authors declare that they have no conflicts of interest.