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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1999-3-25
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pubmed:abstractText |
The red/far-red reversible phytochromes play a central role in regulating the development of plants in relation to their light environment. Studies on the roles of different members of the phytochrome family have mainly focused on light-labile, phytochrome A and light-stable, phytochrome B. Although these two phytochromes often regulate identical responses, they appear to have discrete photosensory functions. Thus, phytochrome A predominantly mediates responses to prolonged far-red light, as well as acting in a non-red/far-red-reversible manner in controlling responses to light pulses. In contrast, phytochrome B mediates responses to prolonged red light and acts photoreversibly under light-pulse conditions. However, it has been reported that rice (Oryza sativa L.) phytochrome A operates in a classical red/far-red reversible fashion following its expression in transgenic tobacco plants. Thus, it was of interest to determine whether transgenic rice phytochrome A could substitute for loss of phytochrome B in phyB mutants of Arabidopsis thaliana (L.) Heynh. We have observed that ectopic expression of rice phytochrome A can correct the reduced sensitivity of phyB hypocotyls to red light and restore their response to end-of-day far-red treatments. The latter is widely regarded as a hallmark of phytochrome B action. However, although transgenic rice phytochrome A can correct other aspects of elongation growth in the phyB mutant it does not restore other responses to end-of-day far-red treatments nor does it restore responses to low red:far-red ratio. Furthermore, transgenic rice phytochrome A does not correct the early-flowering phenotype of phyB seedlings.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PHYA protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/PHYB protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phytochrome,
http://linkedlifedata.com/resource/pubmed/chemical/Phytochrome A,
http://linkedlifedata.com/resource/pubmed/chemical/Phytochrome B,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0032-0935
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
207
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9951735-Arabidopsis,
pubmed-meshheading:9951735-Arabidopsis Proteins,
pubmed-meshheading:9951735-Gene Expression,
pubmed-meshheading:9951735-Hypocotyl,
pubmed-meshheading:9951735-Light,
pubmed-meshheading:9951735-Oryza sativa,
pubmed-meshheading:9951735-Photoreceptor Cells,
pubmed-meshheading:9951735-Phytochrome,
pubmed-meshheading:9951735-Phytochrome A,
pubmed-meshheading:9951735-Phytochrome B,
pubmed-meshheading:9951735-Plants, Genetically Modified,
pubmed-meshheading:9951735-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Overexpression of rice phytochrome A partially complements phytochrome B deficiency in Arabidopsis.
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pubmed:affiliation |
Department of Biology, Leicester University, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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