Global Proteome Turnover Analyses of the Yeasts S. cerevisiae and S. pombe
Open accessAbstract
How cells maintain specific levels of each protein and whether that control is evolutionarily conserved are key questions. Here, we report proteome-wide steady-state protein turnover rate measurements for the evolutionarily distant but ecologically similar yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe. We find that the half-life of most proteins is much longer than currently thought and determined to a large degree by protein synthesis and dilution due to cell division. However, we detect a significant subset of proteins (∼15%) in both yeasts that are turned over rapidly. In addition, the relative abundances of orthologous proteins between the two yeasts are highly conserved across the 400 million years of evolution. In contrast, their respective turnover rates differ considerably. Our data provide a high-confidence resource for studying protein degradation in common yeast model systems.
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The nuances of fluctuation analysis (such as imperfect plating) are frequently disregarded, judging by the continuing popularity of FALCOR.
“To this day the nuances are frequently disregarded, perhaps due to a lack of knowledge, judging by the unfailing popularity of FALCOR (e.g., [67-69]).”
From Efficient, robust, and versatile fluctuation data analysis using MLE MUtation Rate calculator (mlemur) (2023) · cites this paper as [69]
The Introduction and Results describe protein-turnover measurements in yeast, not fluctuation analysis. Searches for FALCOR, imperfect plating, and mutation-rate analysis found no passage addressing the claim or FALCOR’s popularity. (LLM, conf=0.78)
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- Authors
- Christiano, R., Nagaraj, N., Fröhlich, F., & Walther, T. C.
- Affiliations
- Harvard University (US)
- Max Planck Institute of Biochemistry (DE)
- Broad Institute (US)
- Corresponding author
- Walther, Tobias C.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 9
- Issue
- 5
- Pages
- 1959-1965
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC4526151
- OpenAlex
- W1985217551
- Cited by
- 268
- References
- 6
- Citations by year
- 2026: 16 · 2025: 16 · 2024: 16 · 2023: 28 · 2022: 24 · 2021: 27 · 2020: 38 · 2019: 28 · 2018: 27 · 2017: 30 · 2016: 11 · 2015: 7
- FWCI
- 6.56
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Max Planck Digital Library (submittedVersion, other-oa)
- Funders
- National Institute of General Medical Sciences (R01GM095982)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- protein turnover, protein half-life, Saccharomyces cerevisiae, Schizosaccharomyces pombe, protein synthesis, protein degradation, orthologous proteins, evolutionary conservation, proteome-wide analysis
- MeSH terms
- Half-Life, Saccharomyces cerevisiae, Schizosaccharomyces, Proteome, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Proteolysis, Endoplasmic Reticulum-Associated Degradation
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