2009 Fiscal Year Final Research Report
Experimental verification of acquisition of hemoprotein high-order functions by reverse molecular evolution
| 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 |
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Principal Investigator |
IMAI Kiyohiro Hosei University, 生命科学部, 教授 (50028528)
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| 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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| Keywords | ヘム蛋白質 / 分子進化 / 分子設計 / 祖先型 / 遺伝子組換え |
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| 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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[Journal Article] Reduction in hemoglobin-oxygen affinity results in the improvement of exercise capacity in mice with chronic heart failure2008
Author(s)
T. Watanabe, T. Takeda, S. Omiya, S. Hikoso, O. Yamaguchi, Y. Nakano, Y. Higuchi, A. Nakai, Y. Abe, Y. Aki-Jin, M. Taniike, I. Mizote, Y. Matsumura, T. Shimizu, K. Nishida, K. Imai, M. Hori, T. Shirasawa, K. Otsu
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Journal Title
J. Amer. College Cardiol. 52
Pages: 779-786
Peer Reviewed
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