Molecular Diversity of Terpene Synthases in the Liverwort Marchantia polymorpha

Marchantia polymorpha is a basal terrestrial land plant, which like most liverworts accumulates structurally diverse terpenes believed to serve in deterring disease and herbivory. Previous studies have suggested that the mevalonate and methylerythritol phosphate pathways, present in evolutionarily d...

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Published inThe Plant cell Vol. 28; no. 10; pp. 2632 - 2650
Main Authors Kumar, Santosh, Kempinski, Chase, Zhuang, Xun, Norris, Ayla, Mafu, Sibongile, Zi, Jiachen, Bell, Stephen A., Nybo, Stephen Eric, Kinison, Scott E., Jiang, Zuodong, Goklany, Sheba, Linscott, Kristin B., Chen, Xinlu, Jia, Qidong, Brown, Shoshana D., Bowman, John L., Babbitt, Patricia C., Peters, Reuben J., Chen, Feng, Chappell, Joe
Format Journal Article
LanguageEnglish
Published United States American Society of Plant Biologists 01.10.2016
Subjects
Alkyl and Aryl Transferases - genetics
Alkyl and Aryl Transferases - metabolism
Evolution, Molecular
Marchantia - enzymology
Marchantia - genetics
Marchantia - metabolism
Marchantia polymorpha
Transcriptome - genetics
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Summary:Marchantia polymorpha is a basal terrestrial land plant, which like most liverworts accumulates structurally diverse terpenes believed to serve in deterring disease and herbivory. Previous studies have suggested that the mevalonate and methylerythritol phosphate pathways, present in evolutionarily diverged plants, are also operative in liverworts. However, the genes and enzymes responsible for the chemical diversity of terpenes have yet to be described. In this study, we resorted to a HMMER search tool to identify 17 putative terpene synthase genes from M. polymorpha transcriptomes. Functional characterization identified four diterpene synthase genes phylogenetically related to those found in diverged plants and nine rather unusual monoterpene and sesquiterpene synthase-like genes. The presence of separate monofunctional diterpene synthases for ent-copalyl diphosphate and ent-kaurene biosynthesis is similar to orthologs found in vascular plants, pushing the date of the underlying gene duplication and neofunctionalization of the ancestral diterpene synthase gene family to >400 million years ago. By contrast, the mono- and sesquiterpene synthases represent a distinct class of enzymes, not related to previously described plant terpene synthases and only distantly so to microbial-type terpene synthases. The absence of a Mg2+ binding, aspartate-rich, DDXXD motif places these enzymes in a noncanonical family of terpene synthases.
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Current address: College of Pharmacy, Medicinal Chemistry, Ferris State University, Big Rapids, MI 49307.
Current address: School for Engineering of Matter, Transport, and Energy, Arizona State University, Tempe, AZ 85287.
Current address: Department Medicinal Chemistry, University of Utah, Salt Lake, UT 84112.
Current address: Plant Biology Department, University of California, Davis, CA 95616.
Current address: Biotechnology Institute for Chinese Materia Medica, Jinan University, Guangzhou 510632, China.
Current address: Sandia National Laboratory, Livermore, CA 94551-0969.
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions of Authors (www.plantcell.org) is: Joe Chappell (chappell@uky.edu).
Current address: Crops Pathology and Genetics Research Unit, USDA-Agricultural Research Service, Davis, CA 95616.
www.plantcell.org/cgi/doi/10.1105/tpc.16.00062
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.16.00062