Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis
Autor: | Kiyotaka Okada, Tatsuya Sakai, Kensuke Saji, Maki Ohgishi |
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Rok vydání: | 2004 |
Předmět: |
Phototropin
animal structures Light Mutant Restriction Mapping Arabidopsis Receptors G-Protein-Coupled Cryptochrome Biological Clocks Gene Expression Regulation Plant Drosophila Proteins Photosynthesis Receptor Eye Proteins Phototropism Crosses Genetic Oligonucleotide Array Sequence Analysis Genetics Regulation of gene expression Multidisciplinary biology Flavoproteins Arabidopsis Proteins biology.organism_classification Hypocotyl Cell biology Cryptochromes Physical Sciences Photoreceptor Cells Invertebrate sense organs Function (biology) Subcellular Fractions |
Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 101(8) |
ISSN: | 0027-8424 |
Popis: | Blue light receptors in Arabidopsis include two types of proteins, cryptochromes and phototropins. Previous studies have suggested that the cryptochromes cry1 and cry2 function mainly in photomorphogenic responses and that the phototropins phot1 and phot2 mainly regulate photo-induced movements. Receptors in the same family have redundant functions, although their responses to the fluence rate of blue light differ. To uncover functions of blue light receptors that may be concealed by their functional redundancy, we conducted analyses of combinatorial multiple mutants of blue light receptors. Comparison of the responses of the quadruple mutant cry1 cry2 phot1 phot2 to blue light with those of related triple mutants revealed that cryptochromes function in blue light-dependent, random hypocotyl-bending and that phototropins function in one photomorphogenic response, cotyledon expansion. Microarray analysis suggested that cry1 and cry2 independently function as key regulators of early blue light-induced genes, whereas phot1 and phot2 play subsidiary roles in transcriptional regulation by blue light. |
Databáze: | OpenAIRE |
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