Journal
NEW PHYTOLOGIST
Volume 223, Issue 1, Pages 323-335Publisher
WILEY
DOI: 10.1111/nph.15778
Keywords
diterpenoid; Prunella vulgaris (common selfheal); terpene synthase; transcriptome; transit peptide; vulgarisane
Categories
Funding
- Michigan State University Strategic Partnership Grant programme ('Evolutionary-Driven Genome Mining of Plant Biosynthetic Pathways' and 'Plant-inspired Chemical Diversity')
- US Department of Energy-Great Lakes Bioenergy Research Center [DE-FC02-07ER64494, DE-SC0018409]
- Department of Molecular Biology and Biochemistry
- USDA National Institute of Food and Agriculture, HATCH project [MICL02454]
- National Science Foundation [1737898]
- Direct For Biological Sciences
- Division Of Environmental Biology [1737898] Funding Source: National Science Foundation
- U.S. Department of Energy (DOE) [DE-SC0018409] Funding Source: U.S. Department of Energy (DOE)
Ask authors/readers for more resources
The mint family (Lamiaceae) is well documented as a rich source of terpene natural products. More than 200 diterpene skeletons have been reported from mints, but biosynthetic pathways are known for just a few of these. We crossreferenced chemotaxonomic data with publicly available transcriptomes to select common selfheal (Prunella vulgaris) and its highly unusual vulgarisin diterpenoids as a case study for exploring the origins of diterpene skeletal diversity in Lamiaceae. Four terpene synthases (TPS) from the TPS-a subfamily, including two localised to the plastid, were cloned and functionally characterised. Previous examples of TPS-a enzymes from Lamiaceae were cytosolic and reported to act on the 15-carbon farnesyl diphosphate. Plastidial TPS-a enzymes using the 20-carbon geranylgeranyl diphosphate are known from other plant families, having apparently arisen independently in each family. All four new enzymes were found to be active on multiple prenyl-diphosphate substrates with different chain lengths and stereochemistries. One of the new enzymes catalysed the cyclisation of geranylgeranyl diphosphate into 11-hydroxy vulgarisane, the likely biosynthetic precursor of the vulgarisins. We uncovered the pathway to a rare diterpene skeleton. Our results support an emerging paradigm of substrate and compartment switching as important aspects of TPS evolution and diversification.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available