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Plant Cell. 2016 Oct;28(10):2632-2650. Epub 2016 Sep 20.

Molecular Diversity of Terpene Synthases in the Liverwort Marchantia polymorpha.

Author information

1
Plant Biology Program and Department of Pharmaceutical Sciences, University of Kentucky, Lexington, Kentucky 40536-0082.
2
Gradaute School of Genome Science and Technology, University of Tennessee, Knoxville, Tennessee 37996-0840.
3
Roy J. Carver Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011.
4
Department of Plant Sciences, University of Tennessee, Knoxville, Tennessee 37996-4561.
5
Departments of Bioengineering and Therapeutic Sciences and Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158-2330.
6
School of Biological Sciences, Monash University, Melbourne, VIC 3800, Australia.
7
Plant Biology Program and Department of Pharmaceutical Sciences, University of Kentucky, Lexington, Kentucky 40536-0082 chappell@uky.edu.

Abstract

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.

PMID:
27650333
PMCID:
PMC5134972
DOI:
10.1105/tpc.16.00062
[Indexed for MEDLINE]
Free PMC Article

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