AI Article Synopsis
- Researchers used advanced techniques combining BiFC and FRET to study protein interactions in live plant cells.
- They successfully visualized interactions involving three proteins instead of just two, addressing a challenge in the field.
- This innovative method enhances the toolkit for exploring protein interactions in living organisms, potentially benefiting various biological studies.
Article Abstract
Various fluorophore-based microscopic methods, comprising Förster resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC), are suitable to study pairwise interactions of proteins in living cells. The analysis of interactions between more than two protein partners using these methods, however, remains difficult. In this study, we report the successful application of combined BiFC-FRET-fluorescence lifetime imaging microscopy and BiFC-FRET-acceptor photobleaching measurements to visualize the formation of ternary soluble N-ethylmaleimide-sensitive factor attachment receptor complexes in leaf epidermal cells. This method expands the repertoire of techniques to study protein-protein interactions in living plant cells by a procedure capable of visualizing simultaneously interactions between three fluorophore-tagged polypeptide partners.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2832253 | PMC |
| http://dx.doi.org/10.1104/pp.109.151142 | DOI Listing |
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