ArticleYeast (Chichester, England)2014
Identification and characterization of a drug-sensitive strain enables puromycin-based translational assays in Saccharomyces cerevisiae.
Article in Yeast (Chichester, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- The Histone Demethylase JMJD2-Dependent Regulation of rDNA Transcription and Integrity of Nucleolus Is Required for Fungal Development and Pathogenicity in the Rice Blast Fungus.Molecular plant pathology · 2026Article
- Degradation factor 1, Def1, regulates mRNA translation and decay through Ccr4-Not-dependent ubiquitylation of the ribosome.RNA (New York, N.Y.) · 2026Article
- Degradation factor 1, Def1, regulates mRNA translation and decay through Ccr4-Not-dependent ubiquitylation of the ribosome.bioRxiv : the preprint server for biology · 2025Article
- Robustness quantification of a mutant library screen revealed key genetic markers in yeast.Microbial cell factories · 2024Article
- Treatment with surfactants enables quantification of translational activity by O-propargyl-puromycin labelling in yeast.BMC microbiology · 2021Article
- Article
- The science of puromycin: From studies of ribosome function to applications in biotechnology.Computational and structural biotechnology journal · 2020Review
- Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.Molecular cell · 2017Article
- Puromycin- and methotrexate-resistance cassettes and optimized Cre-recombinase expression plasmids for use in yeast.Yeast (Chichester, England) · 2015Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Puromycin is an aminonucleoside antibiotic with structural similarity to aminoacyl tRNA. This structure allows the drug to bind the ribosomal A site and incorporate into nascent polypeptides, causing chain termination, ribosomal subunit dissociation and widespread translational arrest at high concentrations. In contrast, at sufficiently low concentrations, puromycin incorporates primarily at the C-terminus of proteins. While a number of techniques utilize puromycin incorporation as a tool for probing translational activity in vivo, these methods cannot be applied in yeasts that are insensitive to puromycin. Here, we describe a mutant strain of the yeast Saccharomyces cerevisiae that is sensitive to puromycin and characterize the cellular response to the drug. Puromycin inhibits the growth of yeast cells mutant for erg6∆, pdr1∆ and pdr3∆ (EPP) on both solid and liquid media. Puromycin also induces the aggregation of the cytoplasmic processing body component Edc3 in the mutant strain. We establish that puromycin is rapidly incorporated into yeast proteins and test the effects of puromycin on translation in vivo. This study establishes the EPP strain as a valuable tool for implementing puromycin-based assays in yeast, which will enable new avenues of inquiry into protein production and maturation.
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Registered trials
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