Promiscuous terpene synthases from Prunella vulgaris highlight the importance of substrate and compartment switching in terpene synthase evolution

© 2019 The Authors. New Phytologist © 2019 New Phytologist Trust.

Détails bibliographiques
Publié dans:The New phytologist. - 1979. - 223(2019), 1 vom: 01. Juli, Seite 323-335
Auteur principal: Johnson, Sean R (Auteur)
Autres auteurs: Bhat, Wajid Waheed, Sadre, Radin, Miller, Garret P, Garcia, Alekzander Sky, Hamberger, Björn
Format: Article en ligne
Langue:English
Publié: 2019
Accès à la collection:The New phytologist
Sujets:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Prunella vulgaris (common selfheal) diterpenoid terpene synthase transcriptome transit peptide vulgarisane Peptides plus... Polyisoprenyl Phosphates Recombinant Fusion Proteins Terpenes Alkyl and Aryl Transferases EC 2.5.- EC 2.5.1.- geranylgeranyl pyrophosphate N21T0D88LX
Description
Résumé:© 2019 The Authors. New Phytologist © 2019 New Phytologist Trust.
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
Description:Date Completed 11.03.2020
Date Revised 30.09.2020
published: Print-Electronic
GENBANK: NP_176880.1, ACJ38408.1, JX943884.1, KP889115.1, KP889114.1, NM_117823.4, MH926014, MH926015, MH926016, MH926017
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.15778