ArticleScientific reports2021
Comparison of endogenously expressed fluorescent protein fusions behaviour for protein quality control and cellular ageing research.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A versatile dual-color bacterial reporter system highlights two distinctApplied and environmental microbiology · 2026Article
- Feeling the vibes: Vibrational spectroscopic imaging of biomolecular assemblies in their natural environment.Applied physics reviews · 2025Article
- Fluorescent Peptide Tracers for Simultaneous Oxytocin Receptor Activation and Visualization.Angewandte Chemie (International ed. in English) · 2025Article
- Stress-inducible phosphoprotein 1 (Sti1/Stip1/Hop) sequesters misfolded proteins during stress.The FEBS journal · 2025Article
- iPAR: a new reporter for eukaryotic cytoplasmic protein aggregation.BMC methods · 2025Article
- Boosting the toolbox for live imaging of translation.RNA (New York, N.Y.) · 2024Article
- Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The GET pathway is a major bottleneck for maintaining proteostasis in Saccharomyces cerevisiae.Scientific reports · 2023Article
- The Effect of Calorie Restriction on Protein Quality Control in Yeast.Biomolecules · 2023Review
- The Effect of Lithium on the Budding YeastMicroorganisms · 2022Article
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Authors and funding
4 authors.
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Abstract
The yeast Hsp104 protein disaggregase is often used as a reporter for misfolded or damaged protein aggregates and protein quality control and ageing research. Observing Hsp104 fusions with fluorescent proteins is a popular approach to follow post stress protein aggregation, inclusion formation and disaggregation. While concerns that bigger protein tags, such as genetically encoded fluorescent tags, may affect protein behaviour and function have been around for quite some time, experimental evidence of how exactly the physiology of the protein of interest is altered within fluorescent protein fusions remains limited. To address this issue, we performed a comparative assessment of endogenously expressed Hsp104 fluorescent fusions function and behaviour. We provide experimental evidence that molecular behaviour may not only be altered by introducing a fluorescent protein tag but also varies depending on such a tag within the fusion. Although our findings are especially applicable to protein quality control and ageing research in yeast, similar effects may play a role in other eukaryotic systems.
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