Project/Area Number |
12460004
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Breeding science
|
Research Institution | Yokohama City University |
Principal Investigator |
HIRANO Hisashi Yokohama City University, Kihara Institute for Biological Research, Professor, 木原生物学研究所, 教授 (00275075)
|
Co-Investigator(Kenkyū-buntansha) |
SASSA Hidenori Yokohama City University, Kihara Institute for Biological Research, Research Assistant, 木原生物学研究所, 助手 (50295507)
KAWASAKI Hiroshi Yokohama City University, Kihara Institute for Biological Research, Associate Professor, 木原生物学研究所, 助教授 (70169704)
|
Project Period (FY) |
2000 – 2003
|
Project Status |
Completed (Fiscal Year 2003)
|
Budget Amount *help |
¥14,600,000 (Direct Cost: ¥14,600,000)
Fiscal Year 2003: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 2002: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2001: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2000: ¥7,000,000 (Direct Cost: ¥7,000,000)
|
Keywords | Proteome / Protein / Mass spectrometry / Protein function / Post-tranmslational modification / Protein-protein interaction / Seed embryo / Rice / プロテアソーム / 蛋白質機能 / 蛋白質の動態 / プロテインチップ / 機能 / 発芽 / プロテオミクス / 胚芽蛋白質 / ペプチドマスフィンガープリンティング / アミノ酸配列分析 |
Research Abstract |
To analyze efficiently the rice proteome, we developed various analytical techniques in the present study. These include techniques for protein in-gel digestion, peptide mapping, mass spectrometry for identification of proteins separated by two-dimensional electrophoresis, shot-gun analysis of proteins separated by SDS gel electrophoresis, detection for phosphorylated proteins, electrophoresis for high molecular weight proteins, and protein-protein interaction analysis with a novel protein chip. Using the developed techniques, we analyzed comprehensively the rice seed embryo proteome. In this analysis, we identified many proteins without known functions. To obtain the information of functions of these proteins, we performed expression profiling of them, and we identified several proteins, which expressed in relation to germination. On the other hand, we analyzed a large protein complex, 26S proteasome to determine the roles of protein post-translational modifications to obtain fundamental information for proteome analysis. The two-dimensional electrophoresis pattern and the characteristics of individual embryo protein were compiled in our proteome database.
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