• Title/Summary/Keyword: rice proteomics

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Proteome Analysis of the Young Spikelets of Photoperiod-Sensitive Rice Mutant Treated in Different Photoperiods

  • Pandeya, Devendra;Song, You-Chun;Kim, Sung-Su;Suh, Hak-Soo;Kang, Sang-Gu
    • KOREAN JOURNAL OF CROP SCIENCE
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    • 제52권3호
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    • pp.281-288
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    • 2007
  • Photoperiod sensitive genetic male sterile (PGMS) rice is sterile mutant controlled by photoperiod. A PGMS mutant 920S was sterile grown under long-day (LD) photoperiod (14 h light/10 h dark) but fertile grown under short-day (SD) photoperiod (10 h light/14 h dark). Proteome analysis revealed that 12 protein spots were differentially expressed in the spikelets of 920S plants either treated with LD or SD photoperiod. Among these proteins, three proteins including chlorophyll a/b binding protein, vacuolar ATPase ${\beta}-subunit,\;{\alpha}-tubulin$ and an unknown protein were more than three-fold abundant in the spikelet of the SD-treated plants than those of the LD-treated plants. On the other hand, eight proteins including acetyl transferase, 2, 3- biphosphoglycerate, aminopeptidase N, pyruvate decarboxylase, 60S acidic ribosomal protein and three unknown protein spots were more abundant in the spikelets of the LD-treated plants than those of the SD-treated plants. The results suggest that the observed proteins may be involved in sterile or fertile pollen development under LD or SD photoperiod respectively in the PGMS mutant rice.

Physiological and proteomic analysis of young rice leaves grown under nitrogen-starvation conditions

  • Kim, Sang-Gon;Wang, Yiming;Wu, Jingni;Kang, Kyu-Young;Kim, Sun-Tae
    • Plant Biotechnology Reports
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    • 제5권4호
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    • pp.309-315
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    • 2011
  • Rice grown in anaerobic waterlogged soil accumulates ammonium as a major source of nitrogen (N). We have compared the physiological symptoms of rice seedlings subjected to N-starvation stress with those receiving sufficient N, based on measurements of shoot/root length and weight and an analysis of protein expression patterns. N starvation marginally increased root growth but notably decreased shoot biomass. N uptake was reduced by >50% in the roots and shoots of N-starved seedlings. To better understand the mechanism of N starvation in rice, we performed a comparative proteome analysis of proteins isolated from rice leaves. Twenty-five differentially expressed proteins were analyzed by matrixassisted laser desorption/ionization time-of-flight (TOF) mass spectrometry and electron spray ionization quadrupole TOF. Functional analysis of the N-starvation response proteins suggested their involvement in protein synthesis and fate, metabolism, and defense. These results indicate that these proteins may play important roles in regulating the plant's complex adaptation responses for N use during N starvation. The proteins may be useful for further characterization of protein function in plant N nutrition.

Determination of Optimum Rice Harvest Time by Change of the Glutelin Contents During the Maturity Period (벼 등숙기간 중 글루테린 함량 변화에 따른 쌀의 수확적기 판정)

  • Shin, Pyung-Gyun;Chang, An-Cheol;Hong, Seong-Chang;Lee, Ki-Sang;Lee, Keum-Hee;Lee, Yong-Bok
    • Korean Journal of Environmental Agriculture
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    • 제27권4호
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    • pp.460-463
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    • 2008
  • The change of glutelin contents in rice grain during the maturity period was investigated to determine optimum rice harvesting time. The glutelin content was increased with increasing time after heading. In this study, eight of glutelin subunits were found. Among the glutelin subunits, 7208-subunit (MW, 35 kD) contents was significantly increased at 65 days after heading compared with 55 and 60 days after heading. 7405-subunit (MW, 50 kD) contents was steadily increased with time after heading. The results showed that at 55th day after heading would be optimum time for harvest to get the low glutelin content of rice grain.

An Information-based Model for an Interactive Web Service with Agricultural Biotechnology

  • Kim, Chang-Kug;Seo, Young-Joo;Park, Dong-Suk;Hahn, Jang-Ho
    • Genomics & Informatics
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    • 제9권2호
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    • pp.85-88
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    • 2011
  • The National Agricultural Biotechnology Information Center (NABIC) constructed an agricultural biology-based infrastructure and developed a biological information-based database. The major functions of the NABIC are focused on biotechnological developments for agricultural bioinformatics and providing a web-based service to construct bioinformatics workflows easily, such as protein function prediction and genome systems biology programs. The NABIC has concentrated on the functional genomics of major crops, building an integrated biotechnology database for agro-biotech information that focuses on the proteomics of major agricultural resources, such as rice, Chinese cabbage, rice Ds-tagging lines, and microorganisms.

Application of mass-spectrometry compatible photocleavable surfactant for next-generation proteomics using rice leaves (벼의 차세대 단백질체 분석을 위한 질량분석기 호환의 광분해성 계면활성제의 적용)

  • Shin, Hye Won;Nguyen, Truong Van;Jung, Ju Young;Lee, Gi Hyun;Jang, Jeong Woo;Yoon, Jinmi;Gupta, Ravi;Kim, Sun Tae;Min, Cheol Woo
    • Journal of Plant Biotechnology
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    • 제48권3호
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    • pp.165-172
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    • 2021
  • The solubilization of isolated proteins into the adequate buffer containing of surfactants is primary step for proteomic analysis. Particularly, sodium dodecyl sulfate (SDS) is the most widely used surfactant, however, it is not compatible with mass spectrometry (MS). Therefore, it must be removed prior to MS analysis through rigorous washing, which eventually results in inevitable protein loss. Recently, photocleavable surfactant, 4-hexylphenylazosulfonate (Azo), was reported which can be easily degraded by UV irradiation and is compatible with MS during proteomic approach using animal tissues. In this study, we employed comparative label-free proteomic analysis for evaluating the solubilization efficacies of the Azo and SDS surfactants using rice leave proteins. This approach led to identification of 3,365 proteins of which 682 proteins were determined as significantly modulated. Further, according to the subcellular localization prediction in SDS and Azo, proteins localized in the chloroplast were the major organelle accounting for 64% of the total organelle in the SDS sample, while only 37.5% of organelle proteins solubilized in the Azo were predicted to be localized in chloroplast. Taken together, this study validates the efficient solubilization of total protein isolated from plant material for bottom-up proteomics. Azo surfactant is suitable as substitute of SDS and promising for bottom-up proteomics as it facilitates robust protein extraction, rapid washing step during enzymatic digestion, and MS analysis.

Overexpression of a Pathogenesis-Related Protein 10 Enhances Biotic and Abiotic Stress Tolerance in Rice

  • Wu, Jingni;Kim, Sang Gon;Kang, Kyu Young;Kim, Ju-Gon;Park, Sang-Ryeol;Gupta, Ravi;Kim, Yong Hwan;Wang, Yiming;Kim, Sun Tae
    • The Plant Pathology Journal
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    • 제32권6호
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    • pp.552-562
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    • 2016
  • Pathogenesis-related proteins play multiple roles in plant development and biotic and abiotic stress tolerance. Here, we characterize a rice defense related gene named "jasmonic acid inducible pathogenesis-related class 10" (JIOsPR10) to gain an insight into its functional properties. Semi-quantitative RT-PCR analysis showed up-regulation of JIOsPR10 under salt and drought stress conditions. Constitutive over-expression JIOsPR10 in rice promoted shoot and root development in transgenic plants, however, their productivity was unaltered. Further experiments exhibited that the transgenic plants showed reduced susceptibility to rice blast fungus, and enhanced salt and drought stress tolerance as compared to the wild type. A comparative proteomic profiling of wild type and transgenic plants showed that overexpression of JIOsPR10 led to the differential modulation of several proteins mainly related with oxidative stresses, carbohydrate metabolism, and plant defense. Taken together, our findings suggest that JIOsPR10 plays important roles in biotic and abiotic stresses tolerance probably by activation of stress related proteins.

Proteomic analysis of rice mutants susceptible to Magnaporthe oryzae

  • Ryu, Hak-Seung;Song, Min-Young;Kim, Chi-Yeol;Han, Muho;Lee, Sang-Kyu;Ryoo, Nayeon;Cho, Jung-Il;Hahn, Tae-Ryong;Jeon, Jong-Seong
    • Plant Biotechnology Reports
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    • 제3권2호
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    • pp.167-174
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    • 2009
  • To identify genes involved in rice Pi5-mediated disease resistance to Magnaporthe oryzae, we compared the proteomes of the RIL260 rice strain carrying the Pi5 resistance gene with its susceptible mutants M5465 and M7023. Proteins were extracted from the leaf tissues of both RIL260 and the mutant lines at 0, 24, and 48 h after M. oryzae inoculation and separated by two-dimensional polyacrylamide gel electrophoresis (2-DE). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) analysis identified eight proteins that were differently expressed between the resistant and susceptible plants (three down- and five up-regulated proteins in the mutants). The down-regulated proteins included a triosephosphate isomerase (spot no. 2210), a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (no. 3611), and an unknown protein (no. 4505). In addition, the five up-regulated proteins in the mutants were predicted to be a fructokinase I (no. 313), a glutathione S-transferase (no. 2310), an atpB of chloroplast ATP synthase (no. 3616), an aminopeptidase N (no. 3724), and an unknown protein (no. 308). These results suggest that proteomic analysis of rice susceptible mutants is a useful method for identifying novel proteins involved in resistance to the M. oryzae pathogen.

Proteomic Analysis to Identify Tightly-Bound Cell Wall Protein in Rice Calli

  • Cho, Won Kyong;Hyun, Tae Kyung;Kumar, Dhinesh;Rim, Yeonggil;Chen, Xiong Yan;Jo, Yeonhwa;Kim, Suwha;Lee, Keun Woo;Park, Zee-Yong;Lucas, William J.;Kim, Jae-Yean
    • Molecules and Cells
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    • 제38권8호
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    • pp.685-696
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    • 2015
  • Rice is a model plant widely used for basic and applied research programs. Plant cell wall proteins play key roles in a broad range of biological processes. However, presently, knowledge on the rice cell wall proteome is rudimentary in nature. In the present study, the tightly-bound cell wall proteome of rice callus cultured cells using sequential extraction protocols was developed using mass spectrometry and bioinformatics methods, leading to the identification of 1568 candidate proteins. Based on bioinformatics analyses, 389 classical rice cell wall proteins, possessing a signal peptide, and 334 putative non-classical cell wall proteins, lacking a signal peptide, were identified. By combining previously established rice cell wall protein databases with current data for the classical rice cell wall proteins, a comprehensive rice cell wall proteome, comprised of 496 proteins, was constructed. A comparative analysis of the rice and Arabidopsis cell wall proteomes revealed a high level of homology, suggesting a predominant conservation between monocot and eudicot cell wall proteins. This study importantly increased information on cell wall proteins, which serves for future functional analyses of these identified rice cell wall proteins.

Light/Dark Responsiveness of Kinetin-Inducible Secondary Metabolites and Stress Proteins in Rice Leaf

  • Cho, Kyoung-Won;Kim, Dea-Wook;Jung, Young-Ho;Shibato, Junko;Tamogami, Shigeru;Yonekura, Masami;Jwa, Nam-Soo;Kubo, Akihiro;Agrawal, Ganesh Kumar;Rakwal, Randeep
    • Journal of Crop Science and Biotechnology
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    • 제10권2호
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    • pp.112-116
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    • 2007
  • Kinetin(KN) is an inducer of rice(Oryza sativa L.) defense/stress responses, as evidenced by the induction of inducible secondary metabolite and defense/stress protein markers in leaf. We show a novel light-dependent effect of KN-triggered defense stress responses in rice leaf. Leaf segments treated with KN(100 ${\mu}M$) show hypersensitive-like necrotic lesion formation only under continuous light illumination. Potent accumulation of two phytoalexins, sakuranetin and momilactone A(MoA) by KN that peaks at 48 h after treatment under continuous light is completely suppressed by incubation under continuous dark. Using two-dimensional gel electrophoresis we identified KN-induced changes in ribulose-1, 5-bisphosphate carboxylase/oxygenase, energy- and pathogenesis-related proteins(OsPR class 5 and 10 members) by N-terminal amino acid sequencing and mass spectrometry. These changes were light-inducible and could not be observed in the dark(and control). Present results provide a new dimension(light modulation/regulation) to our finding that KN has a potential role in the rice plant self-defense mechanism.

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