Biosynthetic machinery for C25,C25-diether archaeal lipids from the hyperthermophilic archaeon Aeropyrum pernix
- Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi, 464-8601 (Japan)
Highlights: • A. pernix enzymes involved in C25,C25-diether lipid biosynthesis were identified. • Granylfarnesyl reductase catalyzed saturation of C25,C25-diether lipid. • E. coli harboring archaeal genes produced the hyperthermophile-specific lipid. Archaea that thrive in harsh environments usually produce membrane lipids with specific structures such as bipolar tetraether lipids. Only a few genera of archaea, which are hyperthermophiles or halophiles, are known to utilize diether lipids with extended, C{sub 25} isoprenoid hydrocarbon chains. In the present study, we identify two prenyltransferases and a prenyl reductase responsible for the biosynthesis of C{sub 25},C{sub 25}-diether lipids in the hyperthermophilic archaeon Aeropyrum pernix. These enzymes are more specific to C{sub 25} isoprenoid chains than to C{sub 20} chains, which are used for the biosynthesis of ordinary C{sub 20},C{sub 20}-diether archaeal lipids. The recombinant expression of these enzymes with two known archaeal enzymes allows the production of C{sub 25},C{sub 25}-diether archaeal lipids in the cells of Escherichia coli.
- OSTI ID:
- 23137320
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 497, Issue 1; Other Information: Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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