Monolignol ferulate conjugates are naturally incorporated into plant lignins
- Univ. of Wisconsin, Madison, WI (United States). Dept. of Energy Great Lakes Bioenergy Research Center, and Dept. of Biochemistry
- Univ. of Oklahoma, Norman, OK (United States). Dept. of Microbiology and Plant Biology
- Univ. of Wisconsin, Madison, WI (United States). Dept. of Energy Great Lakes Bioenergy Research Center
- Univ. of Auckland, Auckland (New Zealand). School of Biological Sciences, and School of Chemical Sciences
- Univ. of Florida, Wimauma, FL (United States). Dept. of Horticultural Science, Inst. of Food and Agricultural Sciences (IFAS) Gulf Coast Research and Education Center
- Univ. of Auckland, Auckland (New Zealand). School of Chemical Sciences
- Illinois State Univ., Normal, IL (United States). Dept. of Energy Great Lakes Bioenergy Research Center, School of Biological Sciences
- Inst. National de la Recherche Agronomique and AgroParisTech, Inst. Jean-Pierre Bourgin UMR, Versailles (France)
- U.S. Dept. of Agriculture, Madison, WI (United States). U.S. Dairy Forage Research Center, Agricultural Research Service
- Univ. of Wisconsin, Madison, WI (United States). Dept. of Energy Great Lakes Bioenergy Research Center, and Dept. of Biological Systems Engineering
- Samuel Roberts Noble Foundation, Ardmore, OK (United States). Plant Biology Division
- Univ. of Auckland, Auckland (New Zealand). School of Biological Sciences
Angiosperms represent most of the terrestrial plants and are the primary research focus for the conversion of biomass to liquid fuels and coproducts. Lignin limits our access to fibers and represents a large fraction of the chemical energy stored in plant cell walls. Recently, the incorporation of monolignol ferulates into lignin polymers was accomplished via the engineering of an exotic transferase into commercially relevant poplar. We report that various angiosperm species might have convergently evolved to natively produce lignins that incorporate monolignol ferulate conjugates. We show that this activity may be accomplished by a BAHD feruloyl–coenzyme A monolignol transferase, OsFMT1 (AT5), in rice and its orthologs in other monocots.
- Research Organization:
- Univ. of Wisconsin, Madison, WI (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER)
- Grant/Contract Number:
- FC02-07ER64494; AI02-06ER64299
- OSTI ID:
- 1473881
- Journal Information:
- Science Advances, Vol. 2, Issue 10; ISSN 2375-2548
- Publisher:
- AAASCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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