ArticleProtein engineering, design & selection : PEDS2017
A new method for post-translationally labeling proteins in live cells for fluorescence imaging and tracking.
Article in Protein engineering, design & selection : PEDS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Discovery and engineering of retrons for precise genome editing.Nature biotechnology · 2026Article
- A high-affinity split-HaloTag for live-cell protein labeling.Nature communications · 2026Article
- Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Nunchaku: optimally partitioning data into piece-wise contiguous segments.Bioinformatics (Oxford, England) · 2023Article
- Imaging Proteins Sensitive to Direct Fusions Using Transient Peptide-Peptide Interactions.Nano letters · 2023Article
- Uncovering diffusive states of the yeast membrane protein, Pma1, and how labeling method can change diffusive behavior.The European physical journal. E, Soft matter · 2023Article
- PAINT using proteins: A new brush for super-resolution artists.Protein science : a publication of the Protein Society · 2020Review
- Photo-SNAP-tag, a Light-Regulated Chemical Labeling System.ACS chemical biology · 2020Article
- Power to the protein: enhancing and combining activities using the Spy toolbox.Chemical science · 2020Review
- Development of SpyTag/SpyCatcher-Bacmid Expression Vector System (SpyBEVS) for Protein Bioconjugations Inside of Silkworms.International journal of molecular sciences · 2019Article
- Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins.International journal of molecular sciences · 2019Review
- New Routes and Opportunities for Modular Construction of Particulate Vaccines: Stick, Click, and Glue.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
We present a novel method to fluorescently label proteins, post-translationally, within live Saccharomycescerevisiae. The premise underlying this work is that fluorescent protein (FP) tags are less disruptive to normal processing and function when they are attached post-translationally, because target proteins are allowed to fold properly and reach their final subcellular location before being labeled. We accomplish this post-translational labeling by expressing the target protein fused to a short peptide tag (SpyTag), which is then covalently labeled in situ by controlled expression of an open isopeptide domain (SpyoIPD, a more stable derivative of the SpyCatcher protein) fused to an FP. The formation of a covalent bond between SpyTag and SpyoIPD attaches the FP to the target protein. We demonstrate the general applicability of this strategy by labeling several yeast proteins. Importantly, we show that labeling the membrane protein Pma1 in this manner avoids the mislocalization and growth impairment that occur when Pma1 is genetically fused to an FP. We also demonstrate that this strategy enables a novel approach to spatiotemporal tracking in single cells and we develop a Bayesian analysis to determine the protein's turnover time from such data.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.