Lipid Biosynthesis in archaea-Exploring its uniqueness and evolutionary position
| Project/Area Number |
15370049
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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 |
Functional biochemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
NISHINO Tokuzo Tohoku University, Graduate School of Engineering, Professor, 大学院・工学研究科, 教授 (90005827)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAYAMA Toru Tohoku University, Graduate School of Engineering, Associate Professor, 大学院・工学研究科, 助教授 (80268523)
HEMMI Hisashi Tohoku University, Graduate School of Engineering, Assistant Professor, 大学院・工学研究科, 助手 (60302189)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥15,500,000 (Direct Cost: ¥15,500,000)
Fiscal Year 2004: ¥5,200,000 (Direct Cost: ¥5,200,000)
Fiscal Year 2003: ¥10,300,000 (Direct Cost: ¥10,300,000)
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| Keywords | archaea / membrane lipid / biosynthesis / evolution / prenyltransferase / Sulfolobus / geranylgeranylglycerol phosphate / geranylgeranyl diphosphate / アーキア / 脂質生合成 / イソプレノイド / エーテル脂質 / プレニルキノン / ドリコール / イソペンテニルニリン酸 |
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| Research Abstract |
The core structure of membrane lipids of archaea have some unique properties that permit archaea to be distinguished from the others, i.e., bacteria and eukaryotes. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase, which catalyzes the transfer of a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate, is involved in the biosynthesis of archaeal membrane lipids. Enzymes of the UbiA prenyltransferase family are known to catalyze the transfer of a prenyl group to various acceptors with hydrophobic ring structures in the biosynthesis of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin. The thermoacidophilic archaeon S.solfataricus was found to encode three homologues of UbiA prenyltransferase in its genome. One of the homologues encoded by SSO0583 was expressed in Escherichia coli, purified, and characterized. Radioassay and mass spectrometry analysis data indicated that the enzyme specifically catalyzes the biosynthesis of (S)-2,3-di-O-geranylgeranylglyceryl phosphate. The fact that the orthologues of the enzyme are encoded in almost all archaeal genomes clearly indicates the importance of their functions. A phylogenetic tree constructed using the amino acid sequences of some typical members of the UbiA prenyltransferase family and their homologues from S.solfataricus suggests that the two other S.solfataricus homologues, excluding the (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase, are involved in the production of respiratory quinone and heme, respectively. We propose here that archaeal prenyltransferases involved in membrane lipid biosynthesis might be prototypes of the protein family and that archaea might have played an important role in the molecular evolution of prenyltransferases.
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Report
(3 results)
Research Products
(18 results)
