| Project/Area Number |
11440221
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
遺伝
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| Research Institution | OKAYAMA UNIVERSITY (2000-2001)
Hiroshima University (1999) |
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Principal Investigator |
KUTSUKAKE Kazuhiro Okayama University, Faculty of Science, Professor, 理学部, 教授 (90143362)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMAMOTO Tadashi Hiroshima University, Faculty of Applied Biological Science, Associate Professor, 生物生産学部, 助教授 (90187443)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥14,400,000 (Direct Cost: ¥14,400,000)
Fiscal Year 2001: ¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 2000: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1999: ¥9,500,000 (Direct Cost: ¥9,500,000)
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| Keywords | Bacterial flagella / Transcriptional control / Peptidoglycan / Flagellar hook / Posttranscriptional control / Protein export / Export switch / Anti-sigma factor / 殺菌鞭毛 / シグマ因子 / 病原性因子 / 形態形成 / 突然変異体 / 分子集合 / ムラミダーゼ / ペリプラズム / 蛋白質間相互作用 / シャペロン |
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| Research Abstract |
1. FlgJ protein was shown to have a muramidase activity involved in penetration process of the peptidoglycan layer by the rod structure. FlgA was shown to be a periplasmic chaperone essential for P-ring formation.
2. N-terminal one third of the FlgD protein was shown to be involved in modulation of hook assembly, whereas its C terminal portion was found to enhance the translation and export of the hook protein. This suggests that the monitor system of hook completion may depend upon the FlgD-mediated coupling of translation of the hook protein to its export.
3. The FlgM export gate was found to be turned on at the initiation step of hook assembly. This suggests that hook assembly may be carried out with the pool of hook protein which has been already incorporated into the export apparatus by the initiation step of hook assembly.
4. Northern blotting analysis found a 200-base RNA molecule derived from the flgB mRNA. The length of this RNA corresponds to axial length of the basal body-hook structure, suggesting that this RNA may be involved in the hook length control. Expression analysis of the fliC-lacZ translational fusion revealed that its expression is slightly repressed after hook assembly. This suggests that translation-controlling machinery of the fliC gene may be established on hook completion.
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