| Project/Area Number |
15014225
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | University of Tokushima |
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Principal Investigator |
TANIGUCHI Hisaaki University of Tokushima, The Institute for Enzyme Research, Professor, 分子酵素学研究センター, 教授 (10257636)
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| Co-Investigator(Kenkyū-buntansha) |
FUJIWARA Kazuko University of Tokushima, The Institute for Enzyme Research, Assistant professor, 分子酵素学研究センター, 助教授 (20108880)
KONISHI Hiroaki University of Tokushima, The Institute for Enzyme Research, Assistant professor, 分子酵素学研究センター, 助教授 (40252811)
IKEDA Kazuko University of Tokushima, The Institute for Enzyme Research, Assistant, 分子酵素学研究センター, 助手 (10108863)
YAMAUCHI Emiko University of Tokushima, The Institute for Enzyme Research, Assistant, 分子酵素学研究センター, 助手 (50332292)
MATSUZAKI Hideki RIKEN, Posttranslational Modification and Dynamic Regulation Research Team, Researcher, 翻訳後修飾による動的調節機構研究チーム, 連携研究員 (30392129)
岡田 ひとみ 理化学研究所, 翻訳後修飾による動的調節機構研究チーム, 連携研究員
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥50,600,000 (Direct Cost: ¥50,600,000)
Fiscal Year 2004: ¥25,600,000 (Direct Cost: ¥25,600,000)
Fiscal Year 2003: ¥25,000,000 (Direct Cost: ¥25,000,000)
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| Keywords | proteomics / mass spectrometry / signal transduction / informatics / プロテオーム / タンパク質間相互作用 / 蛋白質間相互作用 |
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| Research Abstract |
To conduct large-scale analyses of signal transduction system both by proteomics and bioinformatics, several themes were pursued.
1.A facility for proteomics was established. 2. The facility was used to conduct proteomic analyses of various species including B. subtilis. 3. Analytical methodology was established to conduct differential protein expression analysis, and used for the light-induced change of cyanobacteria. 4.. A new methodology was developed for the isolation of cellular organelles using antibody-bound magnetic beads. The method was used to isolate peroxisomes, and the purified organelle was subjected to proteomic analysis. Among several novel proteins identified, a novel isoform of Lon protease was found to be peroxisome specific. 5. We have established a new method to detect phosphopeptides using triple quadrupole mass spectrometer running in precursor scanning mode. The method was applied for the identification of phosphorylation sites on protein kinase C δ isozyme. Of six phosphorylation sites identified, three tyrosine residues were found to be phosphorylated upon oxidative stress. 6. To analyze the signaling pathways downstream of EGF receptor, tyrosine-phosphorylated proteins were isolated and analyzed by proteomic analysis. Of 150 proteins thus identified, one-third were novel proteins. 7. A large-scale proteomic data containing the sequence data of tryptic peptides were directly mapped onto the raw genome sequence, and the discrepancy between the annotated genome data and proteomic date was compared. Several novel genes in addition to the errors in the raw nucleotide sequence, and wrong annotations of genes were discovered. 8. The 3D structures of several signaling protein and protein complexes were solved, and the detailed mechanisms of modification-regulated protein-protein interaction were elucidated.
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