Cited by 268Ubiquitin and proteasome pathwaysFungal and yeast genetics researchAdvanced Proteomics Techniques and Applications

Global Proteome Turnover Analyses of the Yeasts S. cerevisiae and S. pombe

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Christiano, Romain, Nagaraj, Nagarjuna, Fröhlich, Florian, Walther, Tobias C.·2014·Cell Reports

Abstract

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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Crossref · 10.1016/j.celrep.2014.10.065

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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)
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
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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