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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5394
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pubmed:dateCreated |
1998-12-14
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CRY1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Cryptochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavin Mononucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NPH1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cryptochrome protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1698-701
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9831559-Animals,
pubmed-meshheading:9831559-Arabidopsis,
pubmed-meshheading:9831559-Arabidopsis Proteins,
pubmed-meshheading:9831559-Cell Line,
pubmed-meshheading:9831559-Cryptochromes,
pubmed-meshheading:9831559-Drosophila Proteins,
pubmed-meshheading:9831559-Eye Proteins,
pubmed-meshheading:9831559-Flavin Mononucleotide,
pubmed-meshheading:9831559-Flavoproteins,
pubmed-meshheading:9831559-Genes, Plant,
pubmed-meshheading:9831559-Light,
pubmed-meshheading:9831559-Mutation,
pubmed-meshheading:9831559-Phosphoproteins,
pubmed-meshheading:9831559-Phosphorylation,
pubmed-meshheading:9831559-Photoreceptor Cells, Invertebrate,
pubmed-meshheading:9831559-Phototropism,
pubmed-meshheading:9831559-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9831559-Receptors, G-Protein-Coupled,
pubmed-meshheading:9831559-Recombinant Proteins,
pubmed-meshheading:9831559-Spectrometry, Fluorescence,
pubmed-meshheading:9831559-Spodoptera,
pubmed-meshheading:9831559-Transfection
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pubmed:year |
1998
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pubmed:articleTitle |
Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism.
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pubmed:affiliation |
Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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