ArticleProtoplasma2005
In planta analysis of protein-protein interactions related to light signaling by bimolecular fluorescence complementation.
Article in Protoplasma, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- A quantitative split firefly luciferase complementation assay (SplitLUC) for in planta protein-protein interactions.Protoplasma · 2026Article
- Cellular demiurgs - engineer to understand.Protoplasma · 2026Article
- An optimum study on the laser scanning confocal microscopy techniques for BiFC assay using plant protoplast.Botanical studies · 2024Article
- PoplarInternational journal of molecular sciences · 2020Article
- LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation.The Plant cell · 2019Article
- Protein fragment bimolecular fluorescence complementation analyses for the in vivo study of protein-protein interactions and cellular protein complex localizations.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Article
- A LIM domain protein from tobacco involved in actin-bundling and histone gene transcription.Molecular plant · 2013Article
- An evolutionarily conserved signaling mechanism mediates far-red light responses in land plants.The Plant cell · 2013Article
- Arabidopsis WD repeat domain55 Interacts with DNA damaged binding protein1 and is required for apical patterning in the embryo.The Plant cell · 2012Article
- APC/C-mediated degradation of dsRNA-binding protein 4 (DRB4) involved in RNA silencing.PloS one · 2012Article
- EDL3 is an F-box protein involved in the regulation of abscisic acid signalling in Arabidopsis thaliana.Journal of experimental botany · 2011Article
- MSI4/FVE interacts with CUL4-DDB1 and a PRC2-like complex to control epigenetic regulation of flowering time in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The Arabidopsis CUL4-DDB1 complex interacts with MSI1 and is required to maintain MEDEA parental imprinting.The EMBO journal · 2011Article
- The CRR1 nutritional copper sensor in Chlamydomonas contains two distinct metal-responsive domains.The Plant cell · 2010Article
- Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis.The Plant cell · 2009Article
- A novel shaggy-like kinase interacts with the Tomato leaf curl virus pathogenicity determinant C4 protein.Plant molecular biology · 2009Article
- Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis.The EMBO journal · 2009Article
- Biochemical characterization of Arabidopsis complexes containing CONSTITUTIVELY PHOTOMORPHOGENIC1 and SUPPRESSOR OF PHYA proteins in light control of plant development.The Plant cell · 2008Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The determination of protein-protein interactions is becoming more and more important in the molecular analysis of signal transduction chains. To this purpose the application of a manageable and simple assay in an appropriate biological system is of major concern. Bimolecular fluorescence complementation (BiFC) is a novel method to analyze protein-protein interactions in vivo. The assay is based on the observation that N- and C-terminal subfragments of the yellow-fluorescent protein (YFP) can only reconstitute a functional fluorophore when they are brought into tight contact. Thus, proteins can be fused to the YFP subfragments and the interaction of the fusion proteins can be monitored by epifluorescence microscopy. Pairs of interacting proteins were tested after transient cotransfection in etiolated mustard seedlings, which is a well characterized plant model system for light signal transduction. BiFC could be demonstrated with the F-box protein EID1 (empfindlicher im dunkelroten Licht 1) and the Arabidopsis S-phase kinase-related protein 1 (ASK1). The interaction of both proteins was specific and strictly dependent on the presence of an intact F-box domain. Our studies also demonstrate that etiolated mustard seedlings provide a versatile transient assay system to study light-induced subcellular localization events.
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