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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-5-18
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pubmed:databankReference |
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pubmed:abstractText |
The HY1 locus of Arabidopsis is necessary for phytochrome chromophore biosynthesis and is defined by mutants that show a long hypocotyl phenotype when grown in the light. We describe here the molecular cloning of the HY1 gene by using chromosome walking and mutant complementation. The product of the HY1 gene shows significant similarity to animal heme oxygenases and contains a possible transit peptide for transport to plastids. Heme oxygenase activity was detected in the HY1 protein expressed in Escherichia coli. Heme oxygenase catalyzes the oxygenation of heme to biliverdin, an activity that is necessary for phytochrome chromophore biosynthesis. The predicted transit peptide is sufficient to transport the green fluorescent protein into chloroplasts. The accumulation of the HY1 protein in plastids was detected by using immunoblot analysis with an anti-HY1 antiserum. These results indicate that the Arabidopsis HY1 gene encodes a plastid heme oxygenase necessary for phytochrome chromophore biosynthesis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1288499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1585180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1634523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1644795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1651244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-16593964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-16594056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1674816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1716500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1812812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-1939244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2102834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2111018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2311769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2544027,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2606345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2653818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2753895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2852134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-2901107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-3136167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-3345742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-3394947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-3882712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-429358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-6095209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-6326095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-7744741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-7793979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-7827489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-7872792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-7947784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8049367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8106085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8163179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8175771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8180175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8215388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8288555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8702958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8742713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8755615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8805250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-8901532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10072395-9125512
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
335-48
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:10072395-Amino Acid Sequence,
pubmed-meshheading:10072395-Animals,
pubmed-meshheading:10072395-Arabidopsis,
pubmed-meshheading:10072395-Cloning, Molecular,
pubmed-meshheading:10072395-Gene Expression Regulation, Plant,
pubmed-meshheading:10072395-Heme Oxygenase (Decyclizing),
pubmed-meshheading:10072395-Humans,
pubmed-meshheading:10072395-Molecular Sequence Data,
pubmed-meshheading:10072395-Mutation,
pubmed-meshheading:10072395-Phytochrome,
pubmed-meshheading:10072395-Plants, Genetically Modified,
pubmed-meshheading:10072395-Plastids,
pubmed-meshheading:10072395-Swine
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pubmed:year |
1999
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pubmed:articleTitle |
The Arabidopsis photomorphogenic mutant hy1 is deficient in phytochrome chromophore biosynthesis as a result of a mutation in a plastid heme oxygenase.
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pubmed:affiliation |
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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