| Project/Area Number |
19570222
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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 |
Evolutionary biology
|
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| Research Institution | Hosei University |
|---|
Principal Investigator |
IMAI Kiyohiro Hosei University, 生命科学部, 教授 (50028528)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
TSUNESHIGE Antonio 法政大学, 生命科学部, 教授 (30409346)
NAGAI Masako 金沢大学, 名誉教授 (60019578)
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| Project Period (FY) |
2007 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
|
| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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|---|
| Keywords | ヘム蛋白質 / 分子進化 / 分子設計 / 祖先型 / 遺伝子組換え / ミオグロビン / ヘモグロビン / 祖先型蛋白質 / 逆分子進化 / 進化系統樹 |
|---|
| Research Abstract |
On the basis of the sequence database for proteins now available, we constructed phylogenetic trees for myoglobin and inferred the amino acid sequences for two ancestor animal's myoglobins, one for mammalian and the other for fishes (reverse evolution). These ancestral myoglobins, synthesized in E. coli, showed high oxygen affinity, stable structure and lowered autooxidation rate compared to the corresponding extant neighbor animals, North American opossum and Zebra fish. Thus, it is considered that, in mammals and fishes, myoglobin has evolved so that oxygen binding function is adapted to environments at the sacrifice of structural stability and autooxidation.
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