Visualization and translocation of ternary Calcineurin-A/Calcineurin-B/Calmodulin-2 protein complexes by dual-color trimolecular fluorescence complementation
Fluorescence complementation (FC) techniques are expedient for analyzing bimolecular protein-protein interactions. Here we aimed to develop a method for visualization of ternary protein complexes using dual-color trimolecular fluorescence complementation (TriFC). Dual-color TriFC combines protein fr...
Gespeichert in:
| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
28 April 2015
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| In: |
The new phytologist
Year: 2015, Jahrgang: 208, Heft: 1, Pages: 269-279 |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.13439 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1111/nph.13439 Verlag, lizenzpflichtig, Volltext: https://nph.onlinelibrary.wiley.com/doi/abs/10.1111/nph.13439 
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| Verfasserangaben: | Jan Niklas Offenborn, Rainer Waadt and Jörg Kudla |
MARC
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| 245 | 1 | 0 | |a Visualization and translocation of ternary Calcineurin-A/Calcineurin-B/Calmodulin-2 protein complexes by dual-color trimolecular fluorescence complementation |c Jan Niklas Offenborn, Rainer Waadt and Jörg Kudla |
| 246 | 3 | 3 | |a Visualization and translocation of ternary Calcineurin-A/Calcineurin-B/Calmodulin-two protein complexes by dual-color trimolecular fluorescence complementation |
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| 520 | |a Fluorescence complementation (FC) techniques are expedient for analyzing bimolecular protein-protein interactions. Here we aimed to develop a method for visualization of ternary protein complexes using dual-color trimolecular fluorescence complementation (TriFC). Dual-color TriFC combines protein fragments of mCherry and mVenus, in which a scaffold protein is bilaterally fused to C-terminal fragments of both fluorescent proteins and combined with potential interacting proteins fused to an N-terminal fluorescent protein fragment. For efficient visual verification of ternary complex formation, TriFC was combined with a cytoplasm to plasma membrane translocation assay. Modular vector sets were designed which are fully compatible with previously reported bimolecular fluorescence complementation (BiFC) vectors. As a proof-of-principle, the ternary complex formation of the PP2B protein phosphatase Calcineurin-A/Calcineurin-B with Calmodulin-2 was investigated in transiently transformed Nicotiana benthamiana leaf epidermal cells. The results indicate a Calcineurin-B-induced interaction of Calmodulin-2 with Calcineurin-A. TriFC and the translocation of TriFC complexes provide a novel tool to investigate ternary complex formations with the simplicity of a BiFC approach. The robustness of FC applications and the opportunity to quantify fluorescence complementation render this assay suitable for a broad range of interaction analyses. | ||
| 650 | 4 | |a bimolecular fluorescence complementation (BiFC) | |
| 650 | 4 | |a Calcineurin | |
| 650 | 4 | |a Calmodulin | |
| 650 | 4 | |a fluorescent protein | |
| 650 | 4 | |a interaction analyses | |
| 650 | 4 | |a Nicotiana benthamiana (tobacco) | |
| 650 | 4 | |a protein fragment complementation | |
| 650 | 4 | |a trimolecular fluorescence complementation (TriFC) | |
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