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Proteomic pattern‐based analyses of light responses in Arabidopsis thaliana wild‐type and photoreceptor mutants
Author(s) -
Kim Dong Su,
Cho Dae Shik,
Park WonMan,
Na Hyung Jin,
Nam Hong Gil
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500670
Subject(s) - proteome , arabidopsis thaliana , biology , proteomics , phytochrome , mutant , wild type , arabidopsis , quantitative proteomics , difference gel electrophoresis , two dimensional gel electrophoresis , phytochrome a , biochemistry , botany , gene , red light
Light critically affects the physiology of plants. Using two‐dimensional gel electrophoresis, we used a proteomics approach to analyze the responses of Arabidopsis thaliana to red (660 nm), far‐red (730 nm) and blue (450 nm) light, which are utilized by type II and type I phytochromes, and blue light receptors, respectively. Under specific light treatments, the proteomic profiles of 49 protein spots exhibited over 1.8‐fold difference in protein abundance, significant at p <0.05. Most of these proteins were metabolic enzymes, indicating metabolic changes induced by light of specific wavelengths. The differentially‐expressed proteins formed seven clusters, reflecting co‐regulation. We used the 49 differentially‐regulated proteins as molecular markers for plant responses to light, and by developing a procedure that calculates the Pearson correlation distance of cluster‐to‐cluster similarity in expression changes, we assessed the proteome‐based relatedness of light responses for wild‐type and phytochrome mutant plants. Overall, this assessment was consistent with the known physiological responses of plants to light. However, we also observed a number of novel responses at the proteomic level, which were not predicted from known physiological changes.