Publication Date:
1998-11-30
Description:
The NPH1 gene of Arabidopsis thaliana encodes a 120-kilodalton serine-threonine protein kinase hypothesized to function as a photoreceptor for phototropism. When expressed in insect cells, the NPH1 protein is phosphorylated in response to blue light irradiation. The biochemical and photochemical properties of the photosensitive protein reflect those of the native protein in microsomal membranes. Recombinant NPH1 noncovalently binds flavin mononucleotide, a likely chromophore for light-dependent autophosphorylation. The fluorescence excitation spectrum of the recombinant protein is similar to the action spectrum for phototropism, consistent with the conclusion that NPH1 is an autophosphorylating flavoprotein photoreceptor mediating phototropic responses in higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christie, J M -- Reymond, P -- Powell, G K -- Bernasconi, P -- Raibekas, A A -- Liscum, E -- Briggs, W R -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831559" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Arabidopsis/genetics/*physiology
;
*Arabidopsis Proteins
;
Cell Line
;
Cryptochromes
;
*Drosophila Proteins
;
*Eye Proteins
;
Flavin Mononucleotide/metabolism
;
Flavoproteins/physiology
;
Genes, Plant
;
Light
;
Mutation
;
Phosphoproteins/genetics/*metabolism
;
Phosphorylation
;
*Photoreceptor Cells, Invertebrate
;
*Phototropism
;
Protein-Serine-Threonine Kinases/genetics/*metabolism
;
Receptors, G-Protein-Coupled
;
Recombinant Proteins/metabolism
;
Spectrometry, Fluorescence
;
Spodoptera
;
Transfection
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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