Publication Date:
1999-05-29
Description:
Plants constantly monitor their light environment in order to grow and develop optimally, in part through use of the phytochromes, which sense red/far-red light. A phytochrome binding protein, PKS1 (phytochrome kinase substrate 1), was identified that is a substrate for light-regulated phytochrome kinase activity in vitro. In vivo experiments suggest that PKS1 is phosphorylated in a phytochrome-dependent manner and negatively regulates phytochrome signaling. The data suggest that phytochromes signal by serine-threonine phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fankhauser, C -- Yeh, K C -- Lagarias, J C -- Zhang, H -- Elich, T D -- Chory, J -- R01GM52413/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 28;284(5419):1539-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Howard Hughes Medical Institute, Salk Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10348744" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Arabidopsis/genetics/*metabolism
;
*Arabidopsis Proteins
;
Carrier Proteins/chemistry/genetics/*metabolism
;
Genes, Plant
;
*Intracellular Signaling Peptides and Proteins
;
*Light
;
Molecular Sequence Data
;
Mutation
;
Phosphoproteins/chemistry/genetics/*metabolism
;
Phosphorylation
;
*Photoreceptor Cells
;
Phytochrome/*metabolism
;
Phytochrome A
;
Phytochrome B
;
*Plant Proteins
;
Protein Kinases/metabolism
;
Protein-Serine-Threonine Kinases/metabolism
;
Recombinant Fusion Proteins/metabolism
;
*Signal Transduction
;
*Transcription Factors
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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