ArticleScientific reports2019
The in vivo mechanics of the magnetotactic backbone as revealed by correlative FLIM-FRET and STED microscopy.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Mapping the dynamic plant interactome: from in vitro assays to in vivo quantitative approaches.Plant methods · 2026Review
- A magnetotactic bacterium capable of magnetic sensing.iScience · 2025Article
- Expanding Horizons in Advancements of FRET Biosensing Technologies.Biosensors · 2025Review
- Engineering Magnetotactic Bacteria as Medical Microrobots.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- FRET-FLIM to Determine Protein Interactions and Membrane Topology of Enzyme Complexes.Current protocols · 2022Article
- Through the Eyes of Creators: Observing Artificial Molecular Motors.ACS nanoscience Au · 2022Review
- Combining multiple fluorescence imaging techniques in biology: when one microscope is not enough.Molecular biology of the cell · 2022Article
- A Compass To Boost Navigation: Cell Biology of Bacterial Magnetotaxis.Journal of bacteriology · 2020Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein interaction and protein imaging strongly benefit from the advancements in time-resolved and superresolution fluorescence microscopic techniques. However, the techniques were typically applied separately and ex vivo because of technical challenges and the absence of suitable fluorescent protein pairs. Here, we show correlative in vivo fluorescence lifetime imaging microscopy Förster resonance energy transfer (FLIM-FRET) and stimulated emission depletion (STED) microscopy to unravel protein mechanics and structure in living cells. We use magnetotactic bacteria as a model system where two proteins, MamJ and MamK, are used to assemble magnetic particles called magnetosomes. The filament polymerizes out of MamK and the magnetosomes are connected via the linker MamJ. Our system reveals that bacterial filamentous structures are more fragile than the connection of biomineralized particles to this filament. More importantly, we anticipate the technique to find wide applicability for the study and quantification of biological processes in living cells and at high resolution.
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Registered trials
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