Abstract
To perceive red and far-red light, plants have evolved specific photoreceptors called phytochromes. Even though the spectral properties of all phytochromes are very similar, they show a distinct mode of action. Here we describe EID1, a negatively acting component of the signaling cascade that shifts the responsiveness of the phytochrome A (phyA) signaling system associated with hypocotyl elongation from red to far-red wavelengths. EID1 is a novel nuclear F-box protein that contains a leucine zipper whose integrity is necessary for its biological function. EID1 most probably acts by targeting activated components of the phyA signaling pathway to ubiquitin-dependent proteolysis.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alleles
-
Amino Acid Sequence
-
Arabidopsis Proteins*
-
Base Sequence
-
Cell Nucleus / metabolism
-
Cloning, Molecular
-
DNA-Binding Proteins / chemistry
-
DNA-Binding Proteins / genetics*
-
F-Box Proteins
-
Genes, Recessive
-
Green Fluorescent Proteins
-
Leucine Zippers
-
Light
-
Luminescent Proteins / metabolism
-
Microscopy, Fluorescence
-
Molecular Sequence Data
-
Mutation
-
Nuclear Proteins / chemistry
-
Nuclear Proteins / genetics*
-
Phenotype
-
Phytochrome / genetics*
-
Phytochrome / physiology*
-
Phytochrome A
-
Plant Proteins / metabolism
-
Protein Binding
-
SKP Cullin F-Box Protein Ligases
-
Sequence Homology, Amino Acid
-
Signal Transduction*
-
Tissue Distribution
-
Transformation, Genetic
-
Two-Hybrid System Techniques
Substances
-
ASK1 protein, Arabidopsis
-
Arabidopsis Proteins
-
DNA-Binding Proteins
-
EID1 protein, Arabidopsis
-
F-Box Proteins
-
Luminescent Proteins
-
Nuclear Proteins
-
PHYA protein, Arabidopsis
-
Phytochrome A
-
Plant Proteins
-
Phytochrome
-
Green Fluorescent Proteins
-
ASK2 protein, Arabidopsis
-
SKP Cullin F-Box Protein Ligases