• 제목/요약/키워드: rice proteomics

검색결과 26건 처리시간 0.02초

Proteomics of ionic stresses in rice: An overview

  • Kim, Sang-Gon;Wang, Yiming;Huh, Hyun-Hye;Kim, Yong-Chul;Choi, In-Soo;Agrawal, Ganesh Kumar;Rakwal, Randeep;Kang, Kyu-Young;Kim, Sun-Tae
    • Journal of Plant Biotechnology
    • /
    • 제38권2호
    • /
    • pp.130-136
    • /
    • 2011
  • Ions deficiency or excess remains one of the critical ground level environmental problems, affecting crop productivity. In this overview, we will discuss an increased application of proteomics technology in addressing this issue using rice (Oryza sativa L.) as a model crop plant. Proteomics analyses have revealed that rice proteome undergoes changes in the proteins composition and expression in response to several ionic stresses, including mineral nutrients (aluminum, nitrogen, and phosphorous) and heavy metals (arsenic, cadmium, and copper). Developed inventory of responsive proteins and their correlation with changes in physiological symptoms and parameters are a major step forward in: (i) better understanding the underlying mechanisms of ionic stresses-triggered responses in rice; (ii) comparative proteomics studies; and (iii) designing a novel strategy to improve crop plants.

식물과 곰팡이 병원균과의 상호작용에 대한 프로테오믹스 최근 연구 동향 (Proteomics of plant-fungal pathogen interaction: an overview)

  • 김진영;이소의;오하람;최인수;김용철;김선태
    • Journal of Plant Biotechnology
    • /
    • 제41권1호
    • /
    • pp.1-9
    • /
    • 2014
  • So far it has been generally considered that proteomic approaches are very useful for studying plant-microbes interaction. In this review, recent studies based on papers published from 2010 to 2013 have investigated proteomics analysis in various interaction during plant-fungal pathogen infection by means of gel-based proteomics coupled with mass spectrometry (MS)-based analysis. In rice, three papers focused on rice-Magnaporthe oryzae interaction were mainly reviewed in this study. Interestingly, another study showed proteomic changes in rice inoculated with Puccinia triticina, which is not only an fungal pathogen in wheat and but also results to the disease resistance with non-host defense manner in rice. Additionally, proteomics analysis has been widely subjected to understand defense mechanism during other crops (wheat, tomato, strawberry and mint) and their fungal pathogen interaction. Crops inoculated are analyzed to identify differentially regulated proteins at various tissues such as leaf and apoplast using 2-DE analysis coupled with various MS approaches such as MALDI-TOF MS, nESI-LC-MS/MS and MudPIT, respectively. Taken together, this review article shows that proteomics is applicable to various organisms to understand plant-fungal pathogen interaction and will contribute to provide important information for crop disease diagnosis and crop protection.

작물학 분야 프로테오믹스의 응용과 전망 (Application and perspectives of proteomics in crop science fields)

  • 우선희
    • 한국작물학회:학술대회논문집
    • /
    • 한국작물학회 2004년도 춘계 학술대회지
    • /
    • pp.12-27
    • /
    • 2004
  • Thanks to spectacular advances in the techniques for identifying proteins separated by two-dimensional electrophoresis and in methods for large-scale analysis of proteome variations, proteomics is becoming an essential methodology in various fields of plant sciences. Plant proteomics would be most useful when combined with other functional genomics tools and approaches. A combination of microarray and proteomics analysis will indicate whether gene regulation is controlled at the level of transcription or translation and protein accumulation. In this review, we described the catalogues of the rice proteome which were constructed in our program, and functional characterization of some of these proteins was discussed. Mass-spectrometry is a most prevalent technique to identify rapidly a large of proteins in proteome analysis. However, the conventional Western blotting/sequencing technique us still used in many laboratories. As a first step to efficiently construct protein data-file in proteome analysis of major cereals, we have analyzed the N-terminal sequences of 100 rice embryo proteins and 70 wheat spike proteins separated by two-dimensional electrophoresis. Edman degradation revealed the N-terminal peptide sequences of only 31 rice proteins and 47 wheat proteins, suggesting that the rest of separated protein spots are N-terminally blocked. To efficiently determine the internal sequence of blocked proteins, we have developed a modified Cleveland peptide mapping method. Using this above method, the internal sequences of all blocked rice proteins (i. e., 69 proteins) were determined. Among these 100 rice proteins, thirty were proteins for which homologous sequence in the rice genome database could be identified. However, the rest of the proteins lacked homologous proteins. This appears to be consistent with the fact that about 30% of total rice cDNA have been deposited in the database. Also, the major proteins involved in the growth and development of rice can be identified using the proteome approach. Some of these proteins, including a calcium-binding protein that fumed out to be calreticulin, gibberellin-binding protein, which is ribulose-1,5-bisphosphate carboxylase/oxygenase activate in rice, and leginsulin-binding protein in soybean have functions in the signal transduction pathway. Proteomics is well suited not only to determine interaction between pairs of proteins, but also to identify multisubunit complexes. Currently, a protein-protein interaction database for plant proteins (http://genome .c .kanazawa-u.ac.jp/Y2H)could be a very useful tool for the plant research community. Recently, we are separated proteins from grain filling and seed maturation in rice to perform ESI-Q-TOF/MS and MALDI-TOF/MS. This experiment shows a possibility to easily and rapidly identify a number of 2-DE separated proteins of rice by ESI-Q-TOF/MS and MALDI-TOF/MS. Therefore, the Information thus obtained from the plant proteome would be helpful in predicting the function of the unknown proteins and would be useful in the plant molecular breeding. Also, information from our study could provide a venue to plant breeder and molecular biologist to design their research strategies precisely.

  • PDF

Physiological and Proteomics Analysis to Potassium Starvation in Rice

  • Kim, Sang-Gon;Wang, Yiming;Lee, Chang-Hoon;Chi, Yong-Hun;Kim, Keun-Ki;Choi, In-Soo;Kim, Yong-Chul;Kang, Kyu-Young;Kim, Sun-Tae
    • 한국환경농학회지
    • /
    • 제30권4호
    • /
    • pp.395-401
    • /
    • 2011
  • BACKGROUND: Potassium (K) is one of the macronutrients which are essential for plant growth and development. Its deficiency in paddy soils is becoming one of the limiting factors for increasing rice yield in Asia. METHODS AND RESULTS: To investigate physiological symptoms under K-starvation (NP) compared with complete media (NPK) condition, we measured shoot/root length, weight, nutrients, and patterns of protein expression. The shoot growth was significantly reduced, but root growth was not affected by K-starvation. However, biomasses were decreased in both shoot and root. Uptake of K was reduced up to 85%, while total concentrations of P, Ca, Mg, Na were increased in root and shoot. To better understand the starved K mechanism of rice, comparative proteome analysis for proteins isolated from rice leaves was conducted using 2-DGE. Five spots of differentially expressed proteins were analyzed by MALDI-TOF MS. Analysis of these K-starvation response proteins suggested that they were involved in metabolism and defense. CONCLUSION(s): Physiological and 2-DGE based proteomics approach used in our study results in observation of morphology or nutrients change and identification of K-starvation responsive proteins in rice root. These results have important roles in maintaining nutrient homeostasis and would also be useful for further characterization of protein function in plant K nutrition.

프로테옴 해석에 의한 벼 게놈 기능해석과 응용 (Rice Proteomics: A Functional Analysis of the Rice Genome and Applications)

  • 우선희;김홍식;송범헌;이철원;박영목;정승근;조용구
    • Journal of Plant Biotechnology
    • /
    • 제30권3호
    • /
    • pp.281-291
    • /
    • 2003
  • In this review, we described the catalogues of the rice proteome which were constructed in our program, and functional characterization of some of these proteins was discussed. Mass-spectrometry is the most prevalent technique to rapidly identify a large number of proteome analysis. However, the conventional Western blotting/sequencing technique has been used in many laboratories. As a first step to efficiently construct protein cata-file in proteome analysis of major cereals, we have analyzed the N-terminal sequences of 100 rice embryo proteins and 70 wheat spike proteins separated by two-dimensional electrophoresis. Edman degradation revealed the N-terminal peptide sequences of only 31 rice proteins and 47 wheat proteins, suggesting that the rest of separated protein sports are N-terminally blocked. To efficiently determine the internal sequence of blocked proteins, we have developed a modified Cleveland peptide mapping method. Using this above method, the internal sequences of all blocked rice proteins(i, e., 69 proteins) were determined. Among these 100 rice proteins, thirty were proteins for which homologous sequence in the rice genome database could be identified. However, the rest of the proteins lacked homologous proteins. This appears to be consistent with the fact that about 45% of total rice cDNA have been deposited in the EMBL database. Also, the major proteins involved in the growth and development of rice can be identified using the proteome approach. Some of these proteins, including a calcium-binding protein that tuned out to be calreticulin, gibberellin-binding protein, which is ribulose-1.5-bisphosphate carboxylase/oxygense active in rice, and leginsulin-binding protein in soybean have functions in the signal transduction pathway. Proteomics is well suited not only to determine interaction between pairs of proteins, but also to identify multisubunit complexes. Currently, a protein-protein interaction database for plant proteins(http://genome.c.kanazawa-u.ac.jp/Y2H)could be a very useful tool for the plant research community. Also, the information thus obtained from the plant proteome would be helpful in predicting the function of the unknown proteins and would be useful be in the plant molecular breeding.

벼종자 미랑 단백질의 프로테오믹스 연구를 위한 글루테린 저장 단백질의 제거방법 (A New Removal Method of Glutelin Storage Proteins for the Proteome Study of Non-Glutelin Proteins in Rice Seeds)

  • 우선희;김세영;김태선;조성우;조건;정근욱;김선림;조용구;김홍식;송범헌;이철원;정승근;박영목
    • 한국작물학회지
    • /
    • 제51권spc1호
    • /
    • pp.92-102
    • /
    • 2006
  • 본 연구는 벼종자 미량 단백질의 프로테오믹스 연구를 위하여 벼종자에 고 함량으로 존재하는 벼종자 글루테린 저장 단백질을 제거하는 방법에 관한 것이다. 따라서 본 연구는, (A) 벼종자에 액체 질소를 가하고 분쇄하여 벼종자 가루를 만드는 분쇄단계; (B) 상기 분쇄된 벼종자 가루를 물에 현탁하여 현탁액을 만드는 현탁단계; (C)상기 현탁액 중 미용해 물질을 제거하는 분리단계를 포함하는, 벼종자 미량 단백질의 프로테오믹스 연구를 위한 벼종자 글루테린 저장 단백질의 제거방법에 관하여 검토하였다. 본 연구의 결과, 단순하고 신속하며 저렴하고 효율적인 방법으로 미량 비글루테린 단백질들을 용이하게 동정할 수 있을 것으로 판단되었다.

벼의 등숙에 따른 복합단백질의 post-translational modification 또는 multigene family로 발현하는지? (Multiple spots in 2-D gel : Multigene family or Post-translational Modification in Response to Seed Maturation in Rice ?)

  • 우선희;김세영;김태선;조성우;김진영;조건;정근욱;조용구;이철원;정승근;박영목;최종순
    • 한국작물학회:학술대회논문집
    • /
    • 한국작물학회 2006년도 한국약용작물학회 공동춘계학술발표회
    • /
    • pp.172-173
    • /
    • 2006
  • PDF