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Exploring the response of rice (Oryza sativa) leaf to gibberellins: a proteomic strategy.


ABSTRACT: BACKGROUND:Gibberellins (GAs) are plant-specific hormones that play a central role in the regulation of growth and development with respect to environmental variability. Plants respond to GAs signal through various biochemical and physiological processes. To better understand the response for GA signal, we carried out a proteomic study in rice (Oryza sativa L. spp. japonica) leaf. RESULTS:Through two-dimensional gel electrophoresis (2-DE) and mass spectroscopy analysis, we identified 61 proteins as GA-responsive. These proteins were annotated in various biological functions, such as signal transduction and cell growth/division, photosynthesis and energy metabolism, protein stability and defense. Among these, photosynthetic proteins decreased while many catabolic proteins increased. In addition, GA up-regulated a variety of cell growth/division, protein stability and defense proteins such as cell division cycle protein 48, molecular chaperones, and catalases. CONCLUSION:This is the first report that cell division cycle protein 48 may be responsible for leaf expansion after leaf sensing GA signal. The results presented here provide new insight into the mechanism of rice leaf in response to GA signal.

SUBMITTER: Wang X 

PROVIDER: S-EPMC4883738 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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Exploring the response of rice (Oryza sativa) leaf to gibberellins: a proteomic strategy.

Wang Xiaoqin X   Han Feng F   Yang Mingfeng M   Yang Pingfang P   Shen Shihua S  

Rice (New York, N.Y.) 20130701 1


<h4>Background</h4>Gibberellins (GAs) are plant-specific hormones that play a central role in the regulation of growth and development with respect to environmental variability. Plants respond to GAs signal through various biochemical and physiological processes. To better understand the response for GA signal, we carried out a proteomic study in rice (Oryza sativa L. spp. japonica) leaf.<h4>Results</h4>Through two-dimensional gel electrophoresis (2-DE) and mass spectroscopy analysis, we identif  ...[more]

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