Association of Flavin Adenine Dinucleotide with the Arabidopsis Blue Light Receptor CRY1

The Arabidopsis thaliana HY4 gene encodes CRY1, a 75-kilodalton flavoprotein mediating blue light-dependent regulation of seedling development. CRY1 is demonstrated here to noncovalently bind stoichiometric amounts of flavin adenine dinucleotide (FAD). The redox properties of FAD bound by CRY1 inclu...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1995-08, Vol.269 (5226), p.968-970
Main Authors: Lin, Chentao, Robertson, Dan E., Ahmad, Margaret, Raibekas, Andrei A., Jorns, Marilyn Schuman, Dutton, P. Leslie, Cashmore, Anthony R.
Format: Article
Language:English
Subjects:
Absorption spectra
Analytical, structural and metabolic biochemistry
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins
Arabidopsis thaliana
Biochemistry
Biological and medical sciences
Blue light
Chromophores
Coding
Cryptochromes
Deoxyribodipyrimidine Photo-Lyase - metabolism
DNA
Drosophila Proteins
Environmental aspects
Escherichia coli
Eye Proteins
Feedback (Response)
Flavoproteins
Flavoproteins - chemistry
Flavoproteins - genetics
Flavoproteins - metabolism
Flowers & plants
Fundamental and applied biological sciences. Psychology
Genes
Genes, Plant
Genetic aspects
Holoproteins
Hypocotyls
Inhibition
Light
Monochromatic light
Other proteins
Oxidation-Reduction
Photobiology
Photoreceptor Cells, Invertebrate
Photoreceptors
Photosynthesis
Plant Proteins - chemistry
Plant Proteins - genetics
Plant Proteins - metabolism
Proteins
Quinones - metabolism
Receptors, G-Protein-Coupled
Seedlings
Sequence homology
Spectrum Analysis
Ultraviolet Rays
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The Arabidopsis thaliana HY4 gene encodes CRY1, a 75-kilodalton flavoprotein mediating blue light-dependent regulation of seedling development. CRY1 is demonstrated here to noncovalently bind stoichiometric amounts of flavin adenine dinucleotide (FAD). The redox properties of FAD bound by CRY1 include an unexpected stability of the neutral radical flavosemiquinone (FADH·). The absorption properties of this flavosemiquinone provide a likely explanation for the additional sensitivity exhibited by CRY1-mediated responses in the green region of the visible spectrum. Despite the sequence homology to microbial DNA photolyases, CRY1 was found to have no detectable photolyase activity.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7638620