| Project/Area Number |
11217207
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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 |
Science and Engineering
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| Research Institution | Nagoya University |
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Principal Investigator |
YAMANE Tsuneo Nagoya University, Graduate School of Bio & Agro Sciences, Professor, 大学院・生命農学研究科, 教授 (70026102)
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| Co-Investigator(Kenkyū-buntansha) |
UEDA Shunsaku Utsunomiya University, Faculty of Agriculture, Professor, 農学部, 教授 (80160167)
NAKANO Hideo Nagoya University, Bio-& Agro Sciences, Associate Professor, 大学院・生命農学研究科, 助教授 (00237348)
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| Project Period (FY) |
1999 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥44,500,000 (Direct Cost: ¥44,500,000)
Fiscal Year 2002: ¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 2001: ¥10,500,000 (Direct Cost: ¥10,500,000)
Fiscal Year 2000: ¥11,000,000 (Direct Cost: ¥11,000,000)
Fiscal Year 1999: ¥16,000,000 (Direct Cost: ¥16,000,000)
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| Keywords | PHA / PHB / methylotroph / microbial denitrifyer / Paracoccus denitrificans / phaA / phaR / PHA depolymerase / P(3HB) / P(3HV) / phaP / PHB depolymerase / pha C / pha P / pha R |
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| Research Abstract |
With aim of elucidating regulation mechanism of PHA synthesis/degradation within denitrifyer and methylotroph, Paracoccus denitrificans, studies were carried out on genes/enzymes/metabolism levels, and the following have been achieved.
1. A gene named phaR, was discovered downstream of phaP that encoded PHA granule-associated protein, phasin. PhaR was a transcription factor which bound promoter region of phaP and also bound the PHA granule. It regulated the size of PHA granule.
2. Genes involved in PHA synthesis/degradation, i.e phaA, phaB, phaC, and phaZ, were expressed almost constitutively irrespective of PHA synthesis level.
A metabolite, Coenzyme A, was proposed as a global regulator of PHA biosynthesis.
3. Three enzymes involved in the intracellular degradation of PHA, i.e. two different kinds of PHA depolymerases, and PHB oligomer hydrolase, were purified and their biochemical characteristics were elucidated. One of the PHA depolymerases was a novel enzyme which yielded 3-hydroxylbutyrate monomer directly from PHB polymer.
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