HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain
Details
Serval ID
serval:BIB_2D96CB4AFD5D
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain
Journal
EMBO Journal
ISSN
0261-4189 (Print)
Publication state
Published
Issued date
09/2000
Volume
19
Number
18
Pages
4997-5006
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S. --- Old month value: Sep 15
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S. --- Old month value: Sep 15
Abstract
Arabidopsis HY5 is a bZIP transcription factor that promotes photomorphogenesis. Previous studies suggested that COP1, a negative regulator of photomorphogenesis, directly interacts with nuclear HY5 and targets it for proteasome-mediated degradation. Light negatively regulates the nuclear level of COP1 and thus permits HY5 accumulation. Here we report that HY5 abundance peaks in early seedling development, consistent with its role in promoting photomorphogenesis. HY5 acts exclusively within a complex and exists in two isoforms, resulting from phosphorylation within its COP1 binding domain by a light- regulated kinase activity. Unphosphorylated HY5 shows stronger interaction with COP1, is the preferred substrate for degradation, has higher affinity to target promoters and is physiologically more active than the phosphorylated version. Therefore, HY5 phosphorylation provides an added level of light-mediated regulation of HY5 stability and activity besides nuclear COP1 levels. Regulated HY5 phosphorylation not only provides abundant and physiologically more active unphosphorylated HY5 in the light, but also helps to maintain a small pool of less active phosphorylated HY5 in the dark, which could be essential for a rapid initial response during dark-to-light transition.
Keywords
Amino Acid Sequence
Arabidopsis/*chemistry
*Arabidopsis Proteins
Basic-Leucine Zipper Transcription Factors
Binding Sites
Blotting, Western
Carrier Proteins/chemistry/*metabolism
Casein Kinase II
Cell Nucleus/metabolism
Chromatography, Gel
Glutathione Transferase/metabolism
Light
Molecular Sequence Data
Nuclear Proteins/*chemistry/*genetics/*metabolism
Phosphorylation
Plant Proteins/chemistry/*metabolism
Plants, Genetically Modified
Precipitin Tests
Promoter Regions (Genetics)
Protein Isoforms
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases/metabolism
Recombinant Fusion Proteins/chemistry/metabolism
Sequence Homology, Amino Acid
Time Factors
Tissue Distribution
Transcription Factors/chemistry/metabolism
Transgenes
Two-Hybrid System Techniques
*Ubiquitin-Protein Ligases
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 19:51
Last modification date
20/08/2019 13:12