ArticleFrontiers in plant science2018
Optimizing FRET-FLIM Labeling Conditions to Detect Nuclear Protein Interactions at Native Expression Levels in Living Arabidopsis Roots.
Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Mapping the dynamic plant interactome: from in vitro assays to in vivo quantitative approaches.Plant methods · 2026Review
- FRET-FLIM: Unveiling Transcription Factor Interactions in Plants.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Optimization of FRET imaging in Arabidopsis protoplasts.Molecules and cells · 2025Article
- Article
- One pattern analysis (OPA) for the quantitative determination of protein interactions in plant cells.Plant methods · 2023Article
- FRET-FLIM to Determine Protein Interactions and Membrane Topology of Enzyme Complexes.Current protocols · 2022Article
- Nanosensor Applications in Plant Science.Biosensors · 2022Review
- A PLETHORA/PIN-FORMED/auxin network mediates prehaustorium formation in the parasitic plant Striga hermonthica.Plant physiology · 2022Article
- Visualization of in vivo protein-protein interactions in plants.Journal of experimental botany · 2022Review
- Protoplast: A Valuable Toolbox to Investigate Plant Stress Perception and Response.Frontiers in plant science · 2021Review
- In Vitro Analytical Approaches to Study Plant Ligand-Receptor Interactions.Plant physiology · 2020Review
- Chlamydia-induced curvature of the host-cell plasma membrane is required for infection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Visualizing Protein Associations in Living Arabidopsis Embryo.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Over the rainbow: A practical guide for fluorescent protein selection in plant FRET experiments.Plant direct · 2019Article
- Patterning the Axes: A Lesson from the Root.Plants (Basel, Switzerland) · 2018Review
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
Abstract
Protein complex formation has been extensively studied using Förster resonance energy transfer (FRET) measured by Fluorescence Lifetime Imaging Microscopy (FLIM). However, implementing this technology to detect protein interactions in living multicellular organism at single-cell resolution and under native condition is still difficult to achieve. Here we describe the optimization of the labeling conditions to detect FRET-FLIM in living plants. This study exemplifies optimization procedure involving the identification of the optimal position for the labels either at the N or C terminal region and the selection of the bright and suitable, fluorescent proteins as donor and acceptor labels for the FRET study. With an effective optimization strategy, we were able to detect the interaction between the stem cell regulators SHORT-ROOT and SCARECROW at endogenous expression levels in the root pole of living Arabidopsis embryos and developing lateral roots by FRET-FLIM. Using this approach we show that the spatial profile of interaction between two transcription factors can be highly modulated in reoccurring and structurally resembling organs, thus providing new information on the dynamic redistribution of nuclear protein complex configurations in different developmental stages. In principle, our optimization procedure for transcription factor complexes is applicable to any biological system.
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