Source:http://linkedlifedata.com/resource/pubmed/id/19077168
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2009-5-5
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pubmed:abstractText |
Light is one of the most important environmental factors that regulate plant development. Here we report that a mutation in the Arabidopsis FIERY1 gene (FRY1) caused a shortened hypocotyl and shorter petioles, most dramatically under low-intensity red light and less pronounced under far-red and blue-light conditions. Furthermore, the fry1 mutant flowered late, probably due to a reduced level of FLOWERING LOCUS T (FT) transcript. However, although the transcript level of FRY1 was light-regulated, the chlorophyll level and the expression of typical light-regulated genes were not affected in the fry1 mutant. FRY1 is known as a regulator of abiotic stress responses, and its protein product has dual enzymatic activity comprising inositol polyphosphate-1-phosphatase and 3'(2'),5'-bisphosphate nucleotidase activity. Genetic complementation data obtained using cDNA of the FRY1 paralog AHL (Arabidopsis HAL2-like) and the similar phenotype of an xrn2/xrn3 double mutant suggest that FRY1 attenuates light responses via its 3'(2'),5'-bisphosphate nucleotidase activity rather than its inositol polyphosphate-1-phosphatase activity. We discuss the relationship between the FRY1-associated nucleotidase activity, a step in the pathway for sulfur metabolism and utilization, and the Arabidopsis light response.
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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/Chlorophyll,
http://linkedlifedata.com/resource/pubmed/chemical/FT protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidases,
http://linkedlifedata.com/resource/pubmed/chemical/PHYB protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phytochrome B,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/SAL1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/bisphosphoadenylate 3'-nucleotidase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1365-313X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
208-19
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pubmed:meshHeading |
pubmed-meshheading:19077168-Arabidopsis,
pubmed-meshheading:19077168-Arabidopsis Proteins,
pubmed-meshheading:19077168-Cell Enlargement,
pubmed-meshheading:19077168-Chlorophyll,
pubmed-meshheading:19077168-Flowers,
pubmed-meshheading:19077168-Gene Expression Regulation, Plant,
pubmed-meshheading:19077168-Genes, Plant,
pubmed-meshheading:19077168-Genetic Complementation Test,
pubmed-meshheading:19077168-Light,
pubmed-meshheading:19077168-Mutagenesis, Insertional,
pubmed-meshheading:19077168-Nucleotidases,
pubmed-meshheading:19077168-Phytochrome B,
pubmed-meshheading:19077168-Plants, Genetically Modified,
pubmed-meshheading:19077168-RNA, Plant
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pubmed:year |
2009
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pubmed:articleTitle |
FIERY1 regulates light-mediated repression of cell elongation and flowering time via its 3'(2'),5'-bisphosphate nucleotidase activity.
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pubmed:affiliation |
Department of Biochemistry and Cellular and Molecular Biology, The University of Tennessee, Knoxville, TN 37996-0840, USA.
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pubmed:publicationType |
Journal Article
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