Related Experiment Video
Updated: Apr 19, 2026

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
Published on: November 20, 2017
COP1/SPA ubiquitin ligase complexes repress anthocyanin accumulation under low light and high light conditions
1a Botanical Institute and Cluster of Excellence on Plant Sciences (CEPLAS) ; University of Cologne ; Cologne , Germany.
Abstract:
In Arabidopsis and many other plant species, anthocyanin pigments accumulate only after light exposure and not in darkness. Excess light of very high fluence rates leads to a further, very strong increase in anthocyanin levels. How excess light is sensed is not well understood. Here, we show that mutations in the key repressor of light signaling, the COP1/SPA complex, cause a strong hyperaccumulation of anthocyanins not only under normal light but also under excess, high light conditions. Hence, normal light signaling via COP1/SPA is required to prevent hyperaccumulation of anthocyanins under these high light conditions. However, since cop1 and spa mutants show a similar high-light responsiveness of anthocyanin accumulation as the wild type it remains to be resolved whether COP1/SPA is directly involved in the high-light response itself.
More Related Videos
10:10Investigating Tissue- and Organ-specific Phytochrome Responses using FACS-assisted Cell-type Specific Expression Profiling in Arabidopsis thaliana
Published on: May 29, 2010
09:32Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
Published on: June 15, 2017
Related Concept Videos
Photoreceptors and Plant Responses to Light
The Antenna Complex
Cell Signaling in Plants
Gene Regulation During Sporulation
Biological Clocks and Seasonal Responses
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...