Study of parasite mitochondrial translation system which have truncated functional RNAs
| Project/Area Number |
17590368
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Parasitology (including Sanitary zoology)
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| Research Institution | The University of Tokyo |
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Principal Investigator |
WATANABE Yoh-ichi The University of Tokyo, Graduate School of Medicine, Associate Professor, 大学院医学系研究科, 助教授 (90323568)
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| Co-Investigator(Kenkyū-buntansha) |
OHTSUKI Takashi Okayama University, Faculty of Engineering, Lecturer, 工学部, 講師 (80321735)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2006: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2005: ¥2,600,000 (Direct Cost: ¥2,600,000)
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| Keywords | parasitic nematode / mitochondria / translation / functional RNA / ribosome / tRNA / EF-Tu / nematode |
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| Research Abstract |
Translation system in metazoan mitochondria is quite different from those in eukaryotic cytoplasm and prokaryote in many points. Among those, based on mitochondrial DNA sequences, translation system in nematode mitochondria has been predicted to have shortest tRNAs and shortest rRNA. From the results of analysis of mitochondrial translation system of parasitic and free-living nematodes, we are hoping to reveal that what will happen when functional RNAs in translation system is truncated. In this study, we analyzed these issues and pursued to reveal why truncation of functional RNAs in translation system had happened. We obtained the following results during the last two years:
1.To purify a larger amount of mitochondrial ribosome more efficiently, we prepared recombinant nematode expressing a mitochondrial ribosomal protein with affinity tags. However, we could not obtained mitochondrial ribosome from the transformant, suggesting that optimization of combination of ribosomal protein and tag sequence will be necessary.
2.Using mutant thermophilic bacterial EF-Tu proteins possessing residues found in Caenorhabditis elegans mitochondrial EF-Tu2, we revealed which residues in EF-Tu2 contribute the specificity against seryl-moiety in seryl-tRNA binding.
3.We revealed specificities of aminoacyl-tRNA binding of mitochondrial EF-Tu proteins in parasitic nematode Trichinella spp.
4.We revealed specificities of aminoacyl-tRNA binding of mitochondrial EF-Tu proteins in the arthropod.
5.We found a candidate tRNA methyltransferase.
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Report
(3 results)
Research Products
(26 results)
